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evolution
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co-evolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview
evolution
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coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview
evolution
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coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview
evolution
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coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview
evolution
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During the evolution from cyanobacteria to higher plants, there are significant changes in the localization and function of certain OPS Ndh subunits despite both cyanobacterial and chloroplastic NDH-1 complexes are classified in a same subclass originating from the complex I family, overview. (i) In cyanobacteria, NdhL-NdhN are localized in the middle of membrane-embedded arm and NdhP is included in the membrane arm. In contrast, in higher plants, NdhL-NdhN are localized in the hydrophilic arm and NdhP (NDF6) is a component of subcomplex B, an exclusive NDH-1 subcomplex in higher plants. (ii) In cyanobacteria, the absence of NdhL does not influence the stability and assembly of NDH-1L and NDH-1M complexes although impaired NDH-CET activity and CO2 uptake. In contrast, knockout of ndhL in higher plants results in entire collapse of hydrophilic arm of chloroplastic NDH-1 complex and consequently complete impairment of NDH-CET. (iii) In cyanobacteria, the deletion of ndhO stabilizes NDH-1 complex and increases NDH-CET activity. In higher plants, knockout of ndhO causes complete impairment of NDH-CET and entire collapse of hydrophilic arm of chloroplastic NDH-1 complex. Such opposite effects may be a result of different roles of cyanobacterial and chloroplastic NdhO in coping with environmental stresses. NdhO in cyanobacteria is suggested to be involved in modulating negatively NDH-CET, whereas NdhO in higher plants may mainly participate in stabilizing chloroplast NDH-1 complex. (iv) NdhQ is present in cyanobacteria but its homologue is absent in higher plants. The severe alteration of these OPS Ndh subunits implies significant changes in the activity of cyanobacterial and chloroplastic NDH-1 enzymes during evolution from cyanobacteria to higher plants. In addition, there are more drastic changes in other Ndh subunits during the evolution. In higher plants, Fd has been suggested to be an exclusive electron donor to chloroplast NDH-1, distinctly different from the electron donor of complex I in nonphotosynthetic organisms. In addition to Fd, NADPH may be another potential electron donor in cyanobacterial NDH-1 (cf. EC 7.1.1.11)
evolution
Thermosynechococcus vestitus
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in addition to the NDH-1M module, which is common to all complexes, cyanobacterial NDH-1 complexes differ in the nature of the NdhD and NdhF subunits. Evolution of NDH-1-related protein complexes, overview
evolution
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in addition to the NDH-1M module, which is common to all complexes, cyanobacterial NDH-1 complexes differ in the nature of the NdhD and NdhF subunits. The Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4). Evolution of NDH-1-related protein complexes, overview
evolution
Thermosynechococcus vestitus
NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH. NDH adopts an L-shaped structure that is characteristic of respiratory NADH dehydrogenase complexes
evolution
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NDH-1 complexes belong to the complex I family. On the basis of sequence similarity analysis, the complex I family is suggested to originate from a common ancestor, a group 4 membrane-bound [NiFe] hydrogenase that possesses a proton-transporting hydrogen:ferredoxin (Fd) oxidoreductase activity. During evolution, respiratory NDH-1 and photosynthetic NDH-1 developed different catalytic activities. The former has become equipped with a new NADH-oxidizing module consisting of three subunits and capable of oxidizing NADH, And the latter has retained an original electron input module that accepts electrons from Fd. Structurally, respiratory NDH-1 and photosynthetic NDH-1 contain a conserved L-shaped skeleton
evolution
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NDH-1 is structurally related to respiratory complex I (NADH:ubiquinone oxidoreductase), but unlike the latter, the cyanobacterial enzyme supports cyclic electron flow around photosystem I as well as inorganic carbon uptake via CO2. NDH-1 is also present in plants and algae that harbor the respiratory and photosynthetic machineries in their mitochondria and chloroplasts, respectively. NdhS is homologous to the Src homology 3 domain-like fold found in the ferredoxin-binding site of PSI, and it may thus mediate binding of the electron donor ferredoxin to NDH-1
evolution
Thermosynechococcus vestitus
photosynthetic NDH-1L and respiratory complex I share a conserved L-shaped skeleton and are suggested to originate commonly from a group 4 membrane-bound [NiFe] hydrogenase that accepts electron from ferredoxin (Fd). During evolution, however, respiratory complex I and photosynthetic NDH-1L developed different catalytic reactions. An NADH-binding module consisting of three subunits is capable of oxidizing NADH in the respiratory complex I. But the counterpart of this NADH-binding-module is absent in the photosynthetic NDH-1L complex. The photosynthetic NDH-1L complex retains an original electron input module that accepts electrons from Fd
evolution
Thermosynechococcus vestitus
the cyanobacterial NADPH:plastoquinone oxidoreductase complex (NDH-1) is related to Complex I of eubacteria and mitochondria. At least four different NDH-1 subtypes (NDH-1L, NDH-1L', NDH-1MS, NDH-1MS') have been identified or postulated for cyanobacteria so far. NDH-1L and NDH-1L' are involved in respiration whereas NDH1-MS and NDH-1MS' link the Complex I specific and electron flow dependent proton-pumping activity to unique carbon concentration mechanisms (CCM) in an undefined process. Electron transfer via ferredoxin might be a possible pathway to chloroplast NDH and cyanobacterial NDH-1
evolution
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the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
Thermosynechococcus vestitus
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the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
-
the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
-
the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
-
the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
-
the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria
evolution
Thermosynechococcus vestitus NIES-2133
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photosynthetic NDH-1L and respiratory complex I share a conserved L-shaped skeleton and are suggested to originate commonly from a group 4 membrane-bound [NiFe] hydrogenase that accepts electron from ferredoxin (Fd). During evolution, however, respiratory complex I and photosynthetic NDH-1L developed different catalytic reactions. An NADH-binding module consisting of three subunits is capable of oxidizing NADH in the respiratory complex I. But the counterpart of this NADH-binding-module is absent in the photosynthetic NDH-1L complex. The photosynthetic NDH-1L complex retains an original electron input module that accepts electrons from Fd
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malfunction
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analysis of ndhL deletion mutant (M9) reveals the presence of assembled NDH-1L and NDH-1M complexes, but these complexes appear to be functionally impaired in the absence of NdhL. Both NDH-1 complexes are absent in the ndhB deletion mutant (M55)
malfunction
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deletion of gene ssl0352 impairs cyclic electron transfer (CET) but not the NDH-1 assembly. Deletion of the ssl0352 gene considerably impairs the NDH-CET activity and also retards cell growth under high light conditions, indicating that NdhS is essential for efficient operation of NDH-CET. The high light-dependent phenotype of the two mutants results from defective NDH-CET. But the assembly of the NDH-1L and NDH-1M complexes and their content in the cells are not affected in the mutant. No differences are observed in growth rates and photosynthetic O2 evolution between the wild-type and mutant DELTAssl0352
malfunction
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deletion of NdhQ impairs respiration but not CO2 uptake
malfunction
Thermosynechococcus vestitus
deletion of NdhS causes a similar level of defect in the NDHCET activity as in DELTAndhV cells in response to high-light irradiation
malfunction
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inactivation of ndhB or ndhK results in a high-CO2-requiring phenotype. In cells of the ndhD1/D2 double mutant grown in high CO2, the cyclic electron flow around PSI is strongly impaired and the respiration activity is also low. But cells of this mutant grown at low CO2 show PSI cyclic electron flow similar to wild-type. The donation of electron from NADPH to plastoquinone occurs in thylakoid membranes of wild-type Synechocystis 6803 but is impaired in those of the NdhB-defective mutant
malfunction
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isolation of NDH-CET-defective mutants. Under high-light conditions, the growth of NDH-CET-defective mutants, such as DELTAndhS, is markedly slower in comparison with the wild-type despite similar growth undermoderate light irradiation. Inactivation of cpcG2 impairs NDH-CET activity. Deletion of CpcG2 destabilizes NDH-1L as well as its degradation product NDH-1M and significantly decreases the number of functional photosystem I (PSI) centers, consistent with the involvement of CpcG2 in NDH-1-dependent cyclic electron transport. The CpcG2 deletion, however, has no effect on respiration. The NDH-1L-CpcG2-PSI supercomplex is absent in the cpcG2 deletion mutant, the PSIless mutant, and several other strains deficient in NDH-1L and/or NDH-1M
malfunction
Thermosynechococcus vestitus
NdhP is essential for NDH-1L formation, as this type of NDH-1 is not detectable in a DndhP::Km mutant
malfunction
Thermosynechococcus vestitus NIES-2133
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deletion of NdhS causes a similar level of defect in the NDHCET activity as in DELTAndhV cells in response to high-light irradiation
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metabolism
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biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview
metabolism
Thermosynechococcus vestitus
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biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview
metabolism
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cyanobacterial NADPH:plastoquinone oxidoreductase, or type I NAD(P)H dehydrogenase, or the NDH-1 complex is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I
metabolism
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in wild-type cells the relative amounts of NDH-1 complexes varied depending on growth conditions. The abundant NDH-1M complex was the characteristic feature of cells grown photoautotrophically under air level of CO2. In wild-type cells grown in high CO2 (3%) the relative amount of NDH-1M drastically decreases. NDH-1L, conversely, is slightly upregulated in high CO2-grown cells
metabolism
Thermosynechococcus vestitus
NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis
metabolism
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reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain
metabolism
Thermosynechococcus vestitus
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reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain
metabolism
-
reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain
metabolism
-
reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain
metabolism
-
reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain
metabolism
-
reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain. In Anabaena sp. PCC 7120, the NDH-1 complex is localized to the plasma membrane only
metabolism
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the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I
metabolism
-
the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I
metabolism
-
the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I
metabolism
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the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Two closely related Arabidopsis thaliana proteins, photosynthese-affected-mutant 68 (PAM68) and PAM68-LIKE (PAM68L), are involved in the assembly of the PSII core and of the membrane part of chloroplast NDH-1, respectively. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I
metabolism
Thermosynechococcus vestitus NIES-2133
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NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis
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physiological function
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16 of the 34 editing sites in the Arabidopsis thaliana plastid genome are associated with four ndh genes (ndhB, ndhD, ndhF, and ndhG). Metabolic and physiological functions of NDH-1, overview. In Arabidopsis thaliana ruptured chloroplasts, NADPH-dependent plastoquinone (PQ) reduction by the NDH-1 complex is strictly dependent on the presence of ferredoxin (Fd)
physiological function
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both NDH-1S and NDH-1M are essential for CO2 uptake and that NDH-1M is a functional complex
physiological function
Thermosynechococcus vestitus
cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like complex (NDH) is a key component of this pathway in most oxygenic photosynthetic organisms and is the last large photosynthetic membrane-protein complex. NDH transfers electrons originating from PSI to the plastoquinone pool while pumping protons across the thylakoid membrane, thereby increasing the amount of ATP produced per NADP+ molecule reduced. Mechanism of NDH acquiring and transfering electrons to plastoquinone, overview. The location of the OPS subunits supports a role in electron transfer and defines two potential ferredoxin-binding sites at the apex of the peripheral arm. NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical
physiological function
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metabolic and physiological functions of NDH-1, overview
physiological function
-
metabolic and physiological functions of NDH-1, overview
physiological function
-
metabolic and physiological functions of NDH-1, overview
physiological function
-
metabolic and physiological functions of NDH-1, overview
physiological function
Thermosynechococcus vestitus
-
metabolic and physiological functions of NDH-1, overview
physiological function
-
multisubunit NDH-1 complexes of cyanobacterial are involved in CO2 uptake and cyclic electron transfer (CET) around photosystem I. Protein Ssl0352 (UniProt ID P74795), is another NDH-1 subunit, termed NdhS, in Synechocystis sp. 6803 tightly associated with the NDH-1 complex. Subunit NdhS is important for the function of NDH-1 complexes. NdhS contains a Src homology 3-like domain and might be involved in interaction of the NDH-1 complex with an electron donor. CET produces extra ATP for cell metabolism particularly under stressful conditions. The Ssl0352 protein resides in the thylakoid membrane and associates with the NDH-1L and NDH-1M complexes
physiological function
Thermosynechococcus vestitus
NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress
physiological function
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NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions
physiological function
Thermosynechococcus vestitus
-
NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions
physiological function
-
NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. NdhD1(D2)/NdhF1 are important for both respiration and cyclic electron flow, whereas NdhD3/NdhF3 are responsible for low-CO2-inducible, high-affinity CO2 uptake system, and NdhD4/NdhF4 is involved in a constitutive, low-affinity CO2 uptake. The roles of NdhD5 and NdhD6 are undetermined
physiological function
-
NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. NdhD1(D2)/NdhF1 are important for both respiration and cyclic electron flow, whereas NdhD3/NdhF3 are responsible for low-CO2-inducible, high-affinity CO2 uptake system, and NdhD4/NdhF4 is involved in a constitutive, low-affinity CO2 uptake. The roles of NdhD5 and NdhD6 are undetermined
physiological function
-
NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. Subunit NdhL plays an important role in CO2 uptake and is part of the Synechocystis NDH-1 complex. In contrast to the NdhB, NdhL and NdhK subunits, the ndhH gene is vital to the survival of Synechocystis 6803 even under high-CO2 growth conditions. NDH-1MS is also involved in cyclic electron flow
physiological function
Thermosynechococcus vestitus
photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion
physiological function
Thermosynechococcus vestitus
the cyanobacterial NADPH:plastoquinone oxidoreductase complex (NDH-1) is related to Complex I of eubacteria and mitochondria, it plays a pivotal role in respiration as well as in cyclic electron transfer (CET) around PSI and is involved in a unique carbon concentration mechanism (CCM). NdhP peptide is a unique component of the NDH-1L subtype and essential for its assembly. Electron transfer via ferredoxin might be a possible pathway to chloroplast NDH and cyanobacterial NDH-1
physiological function
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the enzyme commplex participates in a variety of bioenergetic reactions, including respiration, cyclic electron transport around photosystem I and CO2 uptake. Certain role of cyanobacterial and chloroplastic NDH-1 in photosynthetic reactions for the identified sseven OPS subunits of cyanobacterial NDH-1, overview. NdhS might have a common role in binding the reduced Fd from PSI in the catalytic domain of NDH-1 enzymes
physiological function
Thermosynechococcus vestitus
the large size complex of cyanobacterial NAD(P)H dehydrogenase (NDH-1) complex (NDH-1L) plays a crucial role in a variety of bioenergetic reactions such as respiration and cyclic electron flow around photosystem I. The cyanobacterial NDH-1 complex catalyzes the electron transport from reduced ferredoxin (Fd) to plastoquinone via subunits NdhS and NdhH
physiological function
Thermosynechococcus vestitus
the NDH-1MS complex without NdhO is induced to accelerate the NDH-CET activity by long-term high-light irradiation. Enzyme domains and 10 complex components (NdhJ, NdhO, NdhV, NdhI, NdhS, NdhH, NdhM, NdhN, NdhK, and Fd), structure-function relationship, overview
physiological function
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the photosystem I-associated linker protein CpcL, i.e. CpcG2, is essential to stabilize NDH-1L and NDH-1M complexes, interaction analysis of CpcG2 with NDH-1 and PSI complexes. The formation of an NDH-1L-CpcG2-PSI supercomplex in cyanobacteria facilitates photosystem I (PSI) cyclic electron transport via NDH-1L. Cyclic electron transport (CET) around PSI is an important process for oxygenic photosynthetic organisms. In cooperation with linear electron transport, CET contributes to the formation of a proton gradient across the thylakoid membrane, which increases the production of ATP in relation to NADPH and consequently optimizes the ATP/NADPHratio. In addition, CET plays an important role in protecting photosynthesis against various environmental stresses, such as high light. In cyanobacteria, the main route for CET involves NDH-1 complexes, which belong to the complex I family
physiological function
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the two NDH-1 isoforms are involved in redox-driven proton pumping (NDH-1L) and CO2-fixation (NDH-1MS)
physiological function
Thermosynechococcus vestitus NIES-2133
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the NDH-1MS complex without NdhO is induced to accelerate the NDH-CET activity by long-term high-light irradiation. Enzyme domains and 10 complex components (NdhJ, NdhO, NdhV, NdhI, NdhS, NdhH, NdhM, NdhN, NdhK, and Fd), structure-function relationship, overview
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additional information
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determination of the presence of a supercomplex composed of NDH-1, CpcG2, and PSI (NDH-1-CpcG2-PBS-PSI), structure-function relationship and analysis, overview
additional information
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identification of seven oxygenic photosynthesis-specific (OPS) subunits of NDH-1 enzyme, NdhL to NdhQ and NdhS. Six of them are also found in higher plants but not in nonphototrophs. NdhQ appears to be present only in NDH-1L complex. In addition to these subunits, the NDH-1L complex contains NdhD1, NdhF1, NdhP, and NdhQ, and the NDH-1L' complex, which remains elusive, may include NdhD2 and NdhF1. Complex NDH-1S is composed of NdhD3, NdhF3, CupA, and CupS, whereas complex NDH-1S' is made up of NdhD4, NdhF4, and CupB. In Synechocystis sp. 6803, some hydrophilic subunits of wild-type NDH-1 complex, including NdhH-NdhK, NdhN, and NdhO, are copurified with photosystem I (PSI), and several PSI subunits, PsaB-PsaD and PsaF, are copurified with NDH-1
additional information
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NDH-1 is expressed in different isoforms. The NDH-1L and NDH-1L' isoforms support respiration and cyclic electron flow, whereas NDH-1MS and NDH-1MS' are involved in CO2 uptake. Moreover, the NDH-1L' and NDH-1MS' isoforms are constitutive, whereas the NDH-1L and NDH-1MS isoforms are expressed under low CO2 concentrations. All NDH-1 isoforms contain a hydrophilic domain with subunits NdhI/J/K/H harboring three ironsulfur (FeS) centers, N6a, N6b, and N2. In contrast to the respiratory complex I, which receives electrons from NADH via FMN across a ca. 100 A-long chain of 8-9 FeS centers, ferredoxin has been suggested to bind to subunit NdhS, and provide electrons directly to the N6a center. NdhS is homologous to the Src homology 3 domain-like fold found in the ferredoxin-binding site of PSI, and it may thus mediate binding of the electron donor ferredoxin to NDH-1. NDH-1 complex and proton channels structure-function analysis, molecular models of the cyanobacterial NDH-1 showing the NDH-1L isoform and NDH-1MS isoform, homology structure modeling, molecular dynamics simulations, detailed overview
additional information
Thermosynechococcus vestitus
NDH-1L structure modeling, structure-function analysis, overview. Analysis of the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. The hydrophilic arm contains nine NDH subunits, including NdhV and the [4Fe-4S] clusters, the NDH-1L is more rigid in the membrane arm at low pH, whereas the complex is more strongly associated between its two arms at higher pH. NdhV is composed of central loops/beta-strands, which is flanked by the N- and C-terminal helix at one side. In the NDH-Fd structure, NdhV is located above NdhN and NdhS. The central loops/beta-strands of NdhV join with the loops/beta-strands of NdhS, forming strong interactions. In NDH complex, the soluble subunits NdhK and NdhH together with the membrane subunit NdhA play major role in maintaining the association between the membrane and hydrophilic arms. In addition, NdhI, NdhC, and the OPS subunit NdhL also contribute to the interaction between the two arms. The cytoplasmic loop between the first and second TMH (TMH1-2 loop) of NdhC contacts NdhA and the soluble subunits NdhK/NdhH/NdhM, reinforcing the interactions between the two arms. Moreover, the membrane subunit NdhL has a C-terminal fragment projecting into the cytoplasmic region and associating with NdhI/NdhN. While the soluble NdhI possesses an N-terminal amphiphilic helix (N-helix) that embraces the membrane subunits NdhA/NdhL. In addition, three lipid molecules are found at the interface between the two arms, facilitating their association. Two of these lipids link the N-helix of NdhI with the membrane domain of NdhA and NdhC, whereas the third lipid is located in an enclosed cavity formed by the N-terminal fragments from NdhL, NdhN, and NdhK. Pivotal role of lipid molecules in connecting the hydrophilic arm with the membrane arm of the NDH complex
additional information
Thermosynechococcus vestitus
NdhP is a unique component of the 450 kDa NDH-1L complex, that is involved in respiration and CET at high CO2 concentration, and not detectable in the NDH-1MS and NDH-1MS' complexes that play a role in carbon concentration
additional information
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
Thermosynechococcus vestitus
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
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soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview
additional information
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subunit diversity of Ndh-containing complexes, overview
additional information
Thermosynechococcus vestitus
the OPS subunits, specifically NdhS, enable NDH to accept electrons from its electron donor, ferredoxin. Analysis of the arrangement of redox chain and cofactors within the peripheral arm, structure-function analysis, overview
additional information
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the subunit compositions of two types of NAD(P)H dehydrogenase complexes of Synechocystis sp. PCC 6803, NDH-1L and NDH-1M, are analyzed. The NDH-1L complex includes hydrophilic subunits (NdhH, -K, -I, -J, -M, and -N) and hydrophobic subunits (NdhA, -B, -E, -G, -D1, and -F1). In addition, NdhL and a novel subunit, Ssl1690 (designated NdhO), are shown to be components of this complex. All subunits mentioned above are present in the NDH-1M complex except NdhD1 and NdhF1. NdhL and Ssl1690 (NdhO) are homologous to hypothetical proteins encoded by genomic DNA in higher plants, suggesting that chloroplast NDH-1 complexes contain related subunits. N-terminal protein sequencing and mass spectrometry analysis
additional information
Thermosynechococcus vestitus
the yeast two-hybrid system assay confirms the interaction of ferredoxin (Fd) with subunit NdhS and indicates that subunit NdhH is involved in the interaction
additional information
Thermosynechococcus vestitus
X-ray diffraction structure determination at 3.0 A resolution and analysis, modeling, and structure-function analysis, overview. The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. Ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate). A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process
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oligomer
Thermosynechococcus vestitus
the native NDH-1L complex comprises 14 subunits, including the NdhS subunit containing ferredoxin (Fd)-docking site domain
additional information
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the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits.ChloroplastNDH-1includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site
additional information
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the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specificto chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site
additional information
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the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site
additional information
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the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site
additional information
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composition, structure, and membrane localization and topology of the different NDH1 complexes, detailed overview
additional information
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determination of the presence of a supercomplex composed of NDH-1, CpcG2, and PSI (NDH-1-CpcG2-PBS-PSI), structure-function relationship and analysis, overview
additional information
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different NDH-1 complexes are found in the cyanobacterial thylakoid membrane. All of these complexes contain the NDH-1M module, which is composed of both hydrophilic and hydrophobic domains and is presently known to comprise 14 subunits (NdhA-C, NdhE, NdhG-O, and NdhS). NDH-1M has no physiological function by itself but represents an assembly intermediate for functional NDH-1 complexes. The NdhH-K, NdhO, and NdhS subunits form the hydrophilic domain, while the NdhA-C, NdhE, NdhG, and NdhL-N subunits are components of the hydrophobic membrane domain. The NdhO subunit, assigned to the hydrophobic domain, is shown to strongly interact with the NdhI and NdhK subunits of the hydrophilic domain, thereby providing flexibility and maximal NDH-dependent cyclic electron transport (NDH-CET) activity under high-light conditions. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes, as in the case of plant chloroplasts. The maturation factor, the Slr1097 (CRR6) protein, is involved in complex assembly in Synechocystis sp. PCC6803. The Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4)
additional information
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the subunit compositions of two types of NAD(P)H dehydrogenase complexes of Synechocystis sp. PCC 6803, NDH-1L and NDH-1M, are analyzed. The NDH-1L complex includes hydrophilic subunits (NdhH, -K, -I, -J, -M, and -N) and hydrophobic subunits (NdhA, -B, -E, -G, -D1, and -F1). In addition, NdhL and a novel subunit, Ssl1690 (designated NdhO), are shown to be components of this complex. All subunits mentioned above are present in the NDH-1M complex except NdhD1 and NdhF1. N-terminal protein sequencing and mass spectrometry analysis. The subunit composition of NDH-1M is more difficult to access in wild-type cells since the complex overlaps with the PSI monomer and partially with the PSII monomer
additional information
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the the NDH-1 complex is composed of subunits NdhA, NdhB, NdhC, NdhD1, NdhD3, NdhE, NdhF1, NdhF3, NdhG, NdhH, NdhI, NdhJ, and NdhK, plus the ferredoxin binding component NdhS
additional information
Thermosynechococcus vestitus
analysis of the 3.2-A-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from Thermosynechococcus elongatus, NdhS is a constitutive component of NDH-1L and adopts an SH3-like fold, it is the Fd-binding subunit in NDH-1L. But it is unlikely NdhS plays a major role in direct Fd binding, even though the C-terminal 10-residue tail of NdhS is not visible in the EM density. It is more likely that NdhS makes its contribution indirectly as a foothold holding the transient NdhV in the NDH-1L complex for Fd binding. NdhS is required for accumulation of NdhV in the thylakoid membranes but not vice versa. NdhV is a transient subunit of NDH-1L, NdhV can function as an Fd-binding cofactor, guiding the association of Fd to the NDH-1L complex. NdhV may also accelerate the electron transfer rate by helping stabilize the Fd-NdhI interface in an electron transfer-competent conformation. NdhO might be a negative regulator of NDH-CET activity. The Fd-NDH-1L complex structure reveals that all four OPS regulatory subunits are in close vicinity to the electron transport pathway in NDH-1L-NdhL adjacent to the electron acceptor PQ cavity while NdhV, NdhS, and NdhO are at the electron donor Fd-binding site. The peripheral arm of NDH-1L adopts a cylinder-shaped architecture organized by four conserved core subunits (NdhH-NdhK) and two OPS structural subunits (NdhM and NdhN). The central axis of the cylinder is the redox chain of three [4Fe-4S] clusters composed of distal and medial clusters N6a and N6b coordinated in NdhI and terminal cluster. OPS regulatory subunits NdhS, NdhV, and NdhO all fold into small compact structures, binding to the apex of the peripheral arm. NdhS stably sits in a groove of NdhI, holding NdhV to attach to and buttress NdhI for Fd binding and electron transfer. On the opposite side of NdhI, NdhO is secured on the surface of the peripheral arm through interactions with NdhJ, NdhK, and NdhN
additional information
Thermosynechococcus vestitus
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different NDH-1 complexes are found in the cyanobacterial thylakoid membrane. All of these complexes contain the NDH-1M module, which is composed of both hydrophilic and hydrophobic domains and is presently known to comprise 14 subunits (NdhA-C, NdhE, NdhG-O, and NdhS). NDH-1M has no physiological function by itself but represents an assembly intermediate for functional NDH-1 complexes. The NdhH-K, NdhO, and NdhS subunits form the hydrophilic domain, while the NdhA-C, NdhE, NdhG, and NdhL-N subunits are components of the hydrophobic membrane domain. The NdhO subunit, assigned to the hydrophobic domain, is shown to strongly interact with the NdhI and NdhK subunits of the hydrophilic domain, thereby providing flexibility and maximal NDH-dependent cyclic electron transport (NDH-CET) activity under high-light conditions. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes, as in the case of plant chloroplasts
additional information
Thermosynechococcus vestitus
NDH adopts an L-shaped structure that is characteristic of respiratory NADH dehydrogenase complexes. NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH. OPS subunits NdhO and NdhS and the beta-hairpin of core subunit NdhI, surface model, structure-function analysis, overview
additional information
Thermosynechococcus vestitus
several strains of Thermosynechococcus elongatus are constructed by adding a His-tag to different subunits of NDH-1. Two strains with His-tag on CupA and NdhL are successfully used to isolate NDH-1 complexes by one-step Ni2+ column chromatography, revealing the presence of three complexes with molecular masses of about 450, 300 and 190 kDa, which are identified by MS to be NDH-1L, NDH-1M and NDH-1S respectively. A larger complex of about 490 kDa is also isolated from the NdhL-His strain. This complex, designated NDH-1MS, is composed of NDH-1M and NDH-1S (EC 7.1.1.11). The NDH-1L complex is recovered from wild-type cells of Thermosynechococcus elongatus by Ni2+ column chromatography. NdhF1 subunit present only in NDH-1L has a sequence of -HHDHHSHH- internally, which appears to have an affinity for the Ni2+ column. NDH-1S or NDH-1M are not recovered from wild-type cells by chromatography of this kind. The BN/SDS/PAGE analysis of membranes solubilized by a low concentration of detergent indicated the presence of abundant NDH-1MS, but not NDH-1M or NDH-1S. Thus, NDH-1S is associated with NDH-1M in vivo. Selection of the subunit for His tagging is crucial for isolation of NDH-1 complexes
additional information
Thermosynechococcus vestitus
subunit NdhP is essential for stable NDH-1L assembly in Thermosynechococcus elongatus. It is localized in the NDH-1L specific distal unit of the NDH-1 complex, that is formed by the subunits NdhD1 and NdhF1
additional information
Thermosynechococcus vestitus
two structures of NDH-1L from Thermosynechococcus elongatus strain BP-1, in complex with one ferredoxin (Fd) and an endogenous plastoquinone (PQ), respectively. Comparison of NDH-PQ structure (NDHpH7) with previously reported two NDH-1L structures NDHpH6 and NDHpH8 (PDB IDs 6NBY and 6HUM) superposed on NdhA subunit, overview
additional information
Thermosynechococcus vestitus NIES-2133
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analysis of the 3.2-A-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from Thermosynechococcus elongatus, NdhS is a constitutive component of NDH-1L and adopts an SH3-like fold, it is the Fd-binding subunit in NDH-1L. But it is unlikely NdhS plays a major role in direct Fd binding, even though the C-terminal 10-residue tail of NdhS is not visible in the EM density. It is more likely that NdhS makes its contribution indirectly as a foothold holding the transient NdhV in the NDH-1L complex for Fd binding. NdhS is required for accumulation of NdhV in the thylakoid membranes but not vice versa. NdhV is a transient subunit of NDH-1L, NdhV can function as an Fd-binding cofactor, guiding the association of Fd to the NDH-1L complex. NdhV may also accelerate the electron transfer rate by helping stabilize the Fd-NdhI interface in an electron transfer-competent conformation. NdhO might be a negative regulator of NDH-CET activity. The Fd-NDH-1L complex structure reveals that all four OPS regulatory subunits are in close vicinity to the electron transport pathway in NDH-1L-NdhL adjacent to the electron acceptor PQ cavity while NdhV, NdhS, and NdhO are at the electron donor Fd-binding site. The peripheral arm of NDH-1L adopts a cylinder-shaped architecture organized by four conserved core subunits (NdhH-NdhK) and two OPS structural subunits (NdhM and NdhN). The central axis of the cylinder is the redox chain of three [4Fe-4S] clusters composed of distal and medial clusters N6a and N6b coordinated in NdhI and terminal cluster. OPS regulatory subunits NdhS, NdhV, and NdhO all fold into small compact structures, binding to the apex of the peripheral arm. NdhS stably sits in a groove of NdhI, holding NdhV to attach to and buttress NdhI for Fd binding and electron transfer. On the opposite side of NdhI, NdhO is secured on the surface of the peripheral arm through interactions with NdhJ, NdhK, and NdhN
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Peltier, G.; Aro, E.; Shikanai, T.
NDH-1 and NDH-2 plastoquinone reductases in oxygenic photosynthesis
Annu. Plant Biol.
67
55-80
2016
Arabidopsis thaliana, Marchantia polymorpha, Nicotiana tabacum, no activity in Chlamydomonas reinhardtii, Physcomitrium patens, Synechocystis sp. PCC 6803, Thermosynechococcus vestitus
brenda
Zhang, P.; Battchikova, N.; Paakkarinen, V.; Katoh, H.; Iwai, M.; Ikeuchi, M.; Pakrasi, H.B.; Ogawa, T.; Aro, E.M.
Isolation, subunit composition and interaction of the NDH-1 complexes from Thermosynechococcus elongatus BP-1
Biochem. J.
390
513-520
2005
Thermosynechococcus vestitus (Q8DKZ3)
brenda
Saura, P.; Kaila, V.R.I.
Molecular dynamics and structural models of the cyanobacterial NDH-1 complex
Biochim. Biophys. Acta
1860
201-208
2019
Synechocystis sp. PCC 6803
brenda
Ma, W.; Ogawa, T.
Oxygenic photosynthesis-specific subunits of cyanobacterial NADPH dehydrogenases
IUBMB Life
67
3-8
2015
Synechocystis sp. PCC 6803
brenda
Battchikova, N.; Zhang, P.; Rudd, S.; Ogawa, T.; Aro, E.M.
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Thermosynechococcus vestitus (Q8DKZ3)
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