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4Fe-4S cluster
Q97W79; Q97W78; Q97W77; Q97W76
the CCG-domain-containing subunit SdhE (formerly SdhC) contains a [4Fe4S] cluster in reduced (2+) and oxidized (3+) states. The reduced form of the [4Fe4S]2+ cluster is diamagnetic. The individual iron sites of the reduced cluster are noticeably heterogeneous and show partial valence localization, which is particularly strong for one unique ferrous site
iron-sulfur centre
K-edge X-ray absorption spectroscopy is used to monitor the structural changes of their Fe sites in the irreversible [2Fe-2S] cluster degradation process. Regardless of the differences in the cluster-ligating cysteine motifs and the XAS-detectable [2Fe-2S]2+ cluster environments, a complete reductive breakdown of the [2Fe-2S] clusters results in the appearance of a new Fourier transform peak at about 3.3 A with a concomitant loss of the Fe-Fe interaction at ca. 2.7 A for both proteins. The results suggest that a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de novo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
[2Fe-2S]-center
the [2Fe-2S] cluster in SdhB-N and center C in SdhC are two succinate reducible high-potential centers detected in the archaeal succinate:caldariellaquinone oxidoreductase complex that differ in their arrangements of the cluster-binding cysteine motifs and the local cluster surroundings. a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de noVo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
3Fe-4S center
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the iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
3Fe-4S center
sdhB gene encodes an ironsulfur subunit of succinate dehydrogenase
anions
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anions
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required for activity
Ca2+
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activates
Ca2+
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role of calcium cations in the mechanism of phytochrome-dependent regulation of the sdh1-2 gene expression and succinate dehydrogenase activity in maize leaves, overview
Fe
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Fe
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7-8 g-atoms of nonheme iron per 100000 g of protein
Fe
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8 mol nonheme iron per mol of succinate dehydrogenase
Fe
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non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
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4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits
Fe
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3Fe-4S, bound to Ip subunit
Fe
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Fe-S center. Direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
Fe
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non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
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4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits
Fe
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non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
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4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits
Fe-S cluster
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two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol
Fe-S cluster
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at least three distinct types of FeS cluster, at center S-1 a [2Fe-2S]2+,1+ cluster, at center S-2 a [4Fe-4S]2+,1+ cluster, and at center S-3 a [3Fe4S]1+,0 cluster
Fe-S-clusters
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overview
Fe-S-clusters
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electron magnetic resonance study of Fe-S-clusters
Fe-S-clusters
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types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
Fe-S-clusters
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magnetic circular dichroism study of Fe-S-clusters S1-S3
Fe-S-clusters
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types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
Fe-S-clusters
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3Fe-4S centre, bound to Ip subunit
Fe-S-clusters
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4Fe-4S centre, bound to Fp (Fp: flavoprotein subunit, larger) subunit or bridging between Ip and Fp subunits
Fe-S-clusters
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electron magnetic resonance study of Fe-S-clusters
Fe-S-clusters
facultative anaerobic bacterium
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overview
Fe-S-clusters
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contains two 2Fe-2S-centers and one 4Fe-4S-center per mol of histidyl flavin
Fe2+
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in the heme cofactor
Fe2+
of the three iron-sulfur centres bound to subunit Ip, [2Fe-2S] is coordinated by four cysteine residues,B89, B94, B97 and B109, and located in the N-terminal domain, whereas [4Fe-4S] and [3Fe-4S] that are coordinated by four, B182, B185, B188, and B249, and three, B192, B239 and B245, cysteine residues, respectively, are bound to the C-terminal domain. These iron-sulfur centres are also surrounded with highly conserved hydrophobic amino acid residues
Fe2+
within Fe-S clusters
Fe2+
within three Fe-S clusters
Fe2+
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heme cofactor and [3Fe-4S] cluster, midpoint potentials of wild-type and mutant enzymes, overview
Fe2+
within three Fe-S clusters
Fe2+
the protein contains three well-conserved cysteine-rich clusters associated with the iron-sulfur centers involved in electron transport. One of these clusters contains a critical histidine residue implicated in carboxin sensitivity in the basidiomycetes
Fe2+
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the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center, heme b
Fe2+
within Fe-S clusters
Fe2+
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non-heme iron in the iron-sulfur protein in subunit Sdh2p as part of the catalytic dimer of the tetrameric enzyme, and heme iron in a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
Fe2+
iron sulfur subunit of the succinate dehydrogenase protein complex
Fe2+
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in the iron-sulfur protein SdhB and the cytochrome b558, SdhC
Fe2+
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existence of [2Fe-2S], [4Fe-4S] and [3Fe-4S] iron-sulfur clusters within the purified protein, electron paramagnetic resonance spectroscopy, influence of the substrate on the signal corresponding to the [2Fe-2S] cluster, overview
Fe2+
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the enzyme contains a [3Fe-4S] center
Iron
SdhB is the iron-sulfur subunit
Iron
the enzyme complex contains 10 Fe atoms. It contains the canonical centres S1 ([2Fe-2S]+2/+1) and S2 ([4Fe-4S]+2/+1) but lacks centre S3 ([3Fe-4S]+1/0). The iron-sulfur subunit contains an extra cysteine that may allow the binding of a new centre, most probably a tetranuclear one
Iron
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enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes
Iron
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contains [2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters
Iron
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SdhB subunit contains [2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters
Iron
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[2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters in SdhB subunit
Iron
iron-sulfur subunit with 3 distinct [4Fe-4S], [3Fe-3S], and [2Fe-2S] clusters, i.e., organized in 2 domains, all participate in electron transfer, overview
Iron
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Sdh2 subunit contains [2Fe-2S], 4[Fe-4S] and [3Fe-4S] clusters
Iron
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[2Fe-2S], [3Fe-4S] and [4Fe-4S] clusters in Sdh2 subunit
Iron
the enzyme complex contains 102.4 nmol/mg iron
Iron
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attached to menaquinol-oxidising subunit C on the cytoplasmic side of the membrane is subunit B, containing the [3Fe-4S], [4Fe-4S], and [2Fe-2S] iron-sulphur centres (in the order of increasing distance from menaquinol-oxidising subunit C)
Iron
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the iron-sulfur protein of the electron transport phosphorylation system is the donor for fumarate reductase
Iron-sulfur cluster
the enzyme has an unusual iron-sulfur cluster composition with respect to that of the canonical succinate dehydrogenases. Center S3, the succinate responsive [3Fe-4S]1+/0 cluster of succinate dehydrogenases, is not present in membranes prepared from aerobically grown Acidianus ambivalens, nor in partially purified complex fractions. It is replaced by a second [4Fe-4S] center, by incorporation of an additional cysteine, at the cysteine cluster binding motif (CxxYxxCxxxC-->CxxCxxCxxxC). The remaining centers, clusters S1 ([2Fe-2S]1+/2+) and S2 ([4Fe-4S]2+/1+), can be observed
Iron-sulfur cluster
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the enzyme has an unusual iron-sulfur cluster composition with respect to that of the canonical succinate dehydrogenases. Center S3, the succinate responsive [3Fe-4S]1+/0 cluster of succinate dehydrogenases, is not present. The remaining centers, clusters S1 ([2Fe-2S]1+/2+) and S2 ([4Fe-4S]2+/1+), can be observed
Iron-sulfur cluster
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the enzyme has an unusual iron-sulfur cluster composition in respect to that of the canonical succinate dehydrogenases. Center S3, the succinate responsive [3Fe-4S]1+/0 cluster of succinate dehydrogenases, is not present. The remaining centers, clusters S1 ([2Fe-2S]1+/2+) and S2 ([4Fe-4S]2+/1+), can be observed
1.3.5.1 succinate dehydrogenase
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