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x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
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two different stage specific forms of complex II (EC 1.3.5.1) share a comme iron-sulfur subunit
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enzyme consists of a 65000 Da flavoprotein SdhA, a 29000 Da iron-sulfur protein SdhB, and a 19000 Da subunit SdhC containing two b-type cytochromes, SDS-PAGE
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x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
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1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
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1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
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3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
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x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
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? * 62000 + ? * 26000
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x * 70000, flavoprotein of succinate dehydrogenase, SDS-PAGE
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1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
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x * 70000, about, HA-tagged Sdh1p, SDS-PAGE, x * 66000, cleaved HA-tagged Sdh1p, SDS-PAGE
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x * 32000, recombinant SDISP, SDS-PAGE
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x * 32000, recombinant SDISP, SDS-PAGE
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x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
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x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
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x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
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x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
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?
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complex II is comprised of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two transmembrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone
dimer
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1 * 65000 (flavoprotein) + 1 * 28000 (ironprotein) + 19000 (cytochrome protein, membrane anchor), precipitation of radiolabeled protein with specific antibody and SDS-PAGE
dimer
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amino acid sequence around the flavin site
dimer
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two additional polypeptides of 14000 and 15000 are necessary for the two large subunits to associate with the membrane
dimer
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1 * 60000-79000 + 1 * 24000-31000, SDS-PAGE
dimer
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calculation from gene sequence
dimer
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1 * 65000 + 1 * 26000, large subunit is a flavoprotein, small subunit is an iron-sulfur protein
dimer
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1 * 7000 + 1* 27000, SDS-PAGE
dimer
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1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
dimer
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biosynthesis and processing
dimer
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1 * 60000 + 1* 25000, SDS-PAGE
dimer
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amino acid composition of subunits
dimer
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biosynthesis and processing
dimer
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1 * 79000 + 1 * 31000, SDS-PAGE
heterotrimer
determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
heterotrimer
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determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
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heterotrimer
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determination and analysis of the cryo-electronic microscopy structure of trimeric succinate dehydrogenase with the membrane-anchor SdhF at 2.8 A resolution. The membrane-anchored SdhF is a subunit of the enzyme complex II. The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. Within the trimer, each of the three assemblies contains four canonical proteins: an FAD (flavin adenine dinucleotide)-binding protein (SdhA), an iron-sulfur protein (SdhB), and two membrane-anchored proteins (SdhC and SdhD), each with three transmembrane helices
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homodimer
Megalodesulfovibrio gigas
QFR is a homodimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. Two heterotrimeric complexes, each comprising subunits A, B and C, form one stable homodimer (A2B2C2) with major contacts between two C subunit. The formation of the homo-dimer, (A2B2C2), arises from contact of the two C subunits
homodimer
Megalodesulfovibrio gigas DSM 1382
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QFR is a homodimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. Two heterotrimeric complexes, each comprising subunits A, B and C, form one stable homodimer (A2B2C2) with major contacts between two C subunit. The formation of the homo-dimer, (A2B2C2), arises from contact of the two C subunits
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monomer
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1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
monomer
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1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
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oligomer
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homodimeric complex of heterotrimers of A, B, and C subunits
oligomer
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homodimeric complex of heterotrimers of A, B, and C subunits
oligomer
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homodimeric complex of heterotrimers of A, B, and C subunits
tetramer
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the enzyme complex consits of four subunits: a flavoprotein SDH1, an iron-sulfur protein SDH2, two integral membrane subunits SDH3 and SDH4. Protein SDHA F2 is needed for assembly and activity of SDH and also for normal root elongation
tetramer
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1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
tetramer
QFR is composed of Fp, Ip, CybL and CybS subunits
tetramer
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heart, succinate dehydrogenase, SDS-PAGE
tetramer
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amino acid sequence of Ip subunit
tetramer
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1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
tetramer
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succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
tetramer
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fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
tetramer
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secondary structure
tetramer
enzyme QFR is composed of four polypeptide chains, two of which are soluble (flavoprotein, FrdA and iron-sulfur protein, FrdB) and two of which are membrane-spanning (FrdC and FrdD)
tetramer
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1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
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1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
tetramer
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determined by high resolution clear-native electrophoresis and Western blot analysis. Enzyme consists of four subunits: a flavoprotein subunit (Fp, SDH1) and an iron-sulphur subunit (Ip, SDH2) form a soluble heterodimer, which binds to a membrane anchor b-type cytochrome (SDH3)/CybS (SDH4) heterodimer
tetramer
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1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
tetramer
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composed of a catalytic dimer, comprising a flavoprotein subunit Sdh1p and an iron-sulfur protein Sdh2p, and a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
tetramer
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subunits SdhA, SdhB, SdhC, and SdhD
tetramer
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
tetramer
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x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
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tetramer
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4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
tetramer
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4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
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tetramer
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1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
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1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
trimer
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homotrimeric complex of the heterotrimeric protomer
trimer
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trimer of the heterotrimeric protomer. 67000, subunit SdhA, 29000, subunit SdhB, 23000, subunit SdhC, SDS-PAGE
trimer
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1 * 65000-68700, Fp-subunit, FAD-binding, 1 * 27500-28000, Ip-subunit, Fe-S cluster containing, 1 * 19000-22000, membrane binding and cytochrome b containing subunit, SDS-PAGE
trimer
3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis
trimer
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1 * 72000, 1 * 28000, 1 * 14000
trimer
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1 * 72000, 1 * 28000, 1 * 14000
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trimer
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3 * 120000, about, wild-type enzyme, SDS-PAGE
trimer
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the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
trimer
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3 * 120000, about, wild-type enzyme, SDS-PAGE
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trimer
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the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
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trimer
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1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
trimer
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enzyme containing cytochrome b, 1 * 79000 + 1 * 31000 + 1 * 25000
trimer
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1 * 79000 + 1 * 31000 + 1 * 25000
additional information
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SdhC and SdhD form an active complex
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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it is shown that lung stage L3 larvae mitochondria contain larval flavoprotein subunit (Fp) and adult flavoprotein subunit at a ratio of 1:0.56, and that most lung stage L3 larvae cytochrome b containing subunits CybS are of the adult form. This clearly indicates that the rearrangement of complex II begins with a change in the isoform of the anchor CybS subunit, followed by a similar change in the Fp subunit
additional information
the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
additional information
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the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
additional information
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the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
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additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation
additional information
cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation
additional information
succinate:quinone oxidoreductase (SQR) is a multisubunit membrane-associated enzyme. The structure of SdhA is composed of four domains: an FAD-binding domain (residues 1-245 and 351-431), which includes a Rossmann-type fold and provides the binding site for FAD, a capping domain composed of residues 245-351, a helical domain composed of residues 431-547, and a C-terminal domain composed of residues 547-583. The position of the SdhA capping domain is markedly different in the SdhAE assembly relative to SQR, structure comparisons, proposed SdhA assembly pathway, detailed overview. In contrast to the significant structural rearrangements in SdhA, which accompany formation of the SdhAE complex, the structure of SdhE is virtually unchanged
additional information
facultative anaerobic bacterium
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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structure-function relationships of SDH based on the porcine heart enzyme crystal structure, modeling at 2.4 A resolution, PDB ID 1ZOY
additional information
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the catalytic core SdhA and SdhB subunits contain the redox cofactors that participate in electron transfer to ubiquinone. Sdh1 contains the covalently bound FAD cofactor and the binding site for succinate. Sdh2 contains the three Fe-S centers that mediate electron transfer to ubiquinone in the complex of succinate-ubiquinone dehydrogenase, EC 1.3.5.1, regulation of SDH, overview.The membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands
additional information
SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDHA-D (human). The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. SDHB is sandwiched between SDHA on the matrix side, and SDHC and SDHD in the membrane. These two transmembrane subunits thus form the hydrophobic anchor. A small patch of the anchor is exposed on the distal side, to the aqueous intermembrane space. Therefore, the structure of SDH can be divided into two main modules: SDHA and SDHB as the membrane extrinsic (soluble) domain, and SDHC and SDHD as the membrane domain. The interface between the catalytic head domain and the anchor subunits can be separated without the use of detergent, making the catalytic domain an extrinsic membrane protein
additional information
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SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDHA-D (human). The SDHA subunit is a flavoprotein containing a covalently bound FAD cofactor and the binding site for dicarboxylates (e.g. succinate). SDHB is an iron-sulfur cluster protein containing three Fe-S clusters. SDHA and SDHB make up the catalytic domain. They extend out into the matrix and constitute the hydrophilic head. SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them. SDHB is sandwiched between SDHA on the matrix side, and SDHC and SDHD in the membrane. These two transmembrane subunits thus form the hydrophobic anchor. A small patch of the anchor is exposed on the distal side, to the aqueous intermembrane space. Therefore, the structure of SDH can be divided into two main modules: SDHA and SDHB as the membrane extrinsic (soluble) domain, and SDHC and SDHD as the membrane domain. The interface between the catalytic head domain and the anchor subunits can be separated without the use of detergent, making the catalytic domain an extrinsic membrane protein
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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overview on structure, orientation in membranes and genetics
additional information
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structure molecular dynamic simulations using the crystal structure with PDB ID 1PB4
additional information
SDH complex structure and assembly, detailed overview. Succinate dehydrogenase in eukaryotes is composed of four subunits SDH1-4
additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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the enzyme is part of the tetrameric succinate dehydrogenase complex
additional information
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the enzyme is part of the tetrameric succinate dehydrogenase complex
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additional information
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SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
additional information
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SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
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additional information
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SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
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additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
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circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview
additional information
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circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview
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additional information
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classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
additional information
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
additional information
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
additional information
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succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
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