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Enzyme Nomenclature
Information on EC 1.3.5.1 - succinate dehydrogenase
for references in articles please use BRENDA:EC1.3.5.1
Word Map on EC 1.3.5.1
- 1.3.5.1
-
histochemical
- lactate
- fiber
- malate
- paragangliomas
- atpase
-
light-harvesting
- citrate
- glycogen
-
histocompatibility
- isocitrate
- pheochromocytoma
-
tricarboxylic
-
3-nitropropionic
-
germline
- photosystems
- triphosphatase
-
histochemistry
- soleus
-
krebs
-
chlorophyl
-
cytochemical
- lhcii
- aconitase
- thylakoids
- glucose-6-phosphatase
- alpha-ketoglutarate
- huntington
-
bioenergetic
-
mtdna
- gastrocnemius
- rotenone
- striatal
-
vastus
-
gist
- antimycin
- alpha-glycerophosphate
- myofibrillar
-
submitochondrial
- lateralis
- antenna
-
supercomplexes
-
oxphos
-
pdgfra
-
fast-twitch
- neurofibromatosis
- plantaris
-
subsarcolemmal
- hippel-lindau
- biotechnology
-
excitonic
- molecular biology
- diagnostics
- medicine
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.3.5.1
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RECOMMENDED NAME
GeneOntology No.
succinate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinate + a quinone = fumarate + a quinol
-
-
-
-
succinate + a quinone = fumarate + a quinol
can also function as a fumarate reductase
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone).
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CAS REGISTRY NUMBER
COMMENTARY
9002-02-2
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9028-11-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains MRK,Webster, NY8, USG3 and Bridgeport grown in HL-60 cells, genes sdhA, sdhB, sdhC and sdhD
-
-
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
B1YBY7: flavoprotein subunit, B1YBY8: ferredoxin
B1YBY7, B1YBY8
UniProt
B1YBY7: flavoprotein subunit, B1YBY8: ferredoxin
B1YBY7, B1YBY8
UniProt
gene SDH2-2, encoding the iron sulfur subunit of the succinate dehydrogenase protein complex
D2KQI9
UniProt
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
UniProt
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, P77946: subunit sdhD
UniProt
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
O73937: FAD-containing subunit SdhA, O73937: iron-sulfur subunit SdhB, O73939: subunit SdhC, O73940: subunit SdhD
SwissProt
succinate dehydrogenase
2877, 391082, 391117, 391120, 391123, 391124, 391130, 391136, 391146, 391165, 391179, 391180, 391185
-
-
-
391083, 391091, 391099, 391140, 391149, 391154, 391169, 391170, 391171, 391172, 391173, 391184, 391185, 391191, 654092, 655573, 656003, 656090, 657349, 671813, 674478, 674634, 674644, 674678, 674762, 685281, 695359, 696480, 698668, 698946, 708966
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-
-
654444, 656605, 686169, 686171, 686519, 686995, 687015, 687923, 687955, 687965, 687966, 687968, 688213, 688882, 688964, 689710, 697001, 697078, 697362, 697618, 697623, 698179, 700139, 711232, 712976, 724698, 741795
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-
isoform Sdh1 is encoded by a five-gene operon. A0QPJ1 i.e. gene MSMEG_0416, A0QPJ2 i.e. gene MSMEG_0417, A0QPJ3 i.e. gene MSMEG_0418, A0QPJ4 i.e. gene MSMEG_0419, A0QPJ5 i.e. gene MSMEG_0420
A0QPJ1, A0QPJ2, A0QPJ3, A0QPJ4, A0QPJ5
UniProt
isoform Sdh2 is encoded by a five-gene operon. A0QT07 i.e. gene MSMEG_1669, A0QT08 i.e. gene MSMEG_1670, A0QT09 i.e. gene MSMEG_1671, A0QT10 i.e. gene MSMEG_1672
UniProt
isoform Sdh1 is encoded by a five-gene operon. A0QPJ1 i.e. gene MSMEG_0416, A0QPJ2 i.e. gene MSMEG_0417, A0QPJ3 i.e. gene MSMEG_0418, A0QPJ4 i.e. gene MSMEG_0419, A0QPJ5 i.e. gene MSMEG_0420
A0QPJ1, A0QPJ2, A0QPJ3, A0QPJ4, A0QPJ5
UniProt
isoform Sdh2 is encoded by a five-gene operon. A0QT07 i.e. gene MSMEG_1669, A0QT08 i.e. gene MSMEG_1670, A0QT09 i.e. gene MSMEG_1671, A0QT10 i.e. gene MSMEG_1672
UniProt
-
391081, 391140, 391191, 654172, 657158, 673796, 674053, 677203, 685306, 688533, 689109, 695601, 698668, 699137
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flavoprotein subunit of thr succinate dehydrogenase; gene sdhA
UniProt
-
391115, 391140, 391183, 391191, 654819, 655999, 656178, 656275, 656276, 672406, 698179, 698817, 725497
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-
genes SDHA, SDHB, SDHC, and SDHD encding the four subunits of the enzyme
-
-
Q97W79: subunit sdhA, Q97W78: subunit sdhB, Q97W77: subunit sdhE (formerly SdhC), Q97W76: subunit sdhD
Q97W79, Q97W78, Q97W77, Q97W76
UniProt
Q97W79: subunit sdhA, Q97W78: subunit sdhB, Q97W77: subunit sdhE (formerly SdhC), Q97W76: subunit sdhD
Q97W79, Q97W78, Q97W77, Q97W76
UniProt
F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
UniProt
F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
UniProt
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase
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-
formerly Vibrio succinogenes, fumarate reductase; succinate dehydrogenase
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
enzymatic activity, quinone content and complex II subunit composition in mitochondria of lung stage L3 (LL3) Ascaris suum larvae is examined. Lung stage L3 Ascaris suum larvae mitochondria show higher quinol–fumarate reductase activity than mitochondria of Ascaris suum at other stages. Ubiquinone content in lung stage L3 larvae mitochondria is more abundant than rhodoquinone. 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
physiological function
additional information
evolution
-
the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases
evolution
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases
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malfunction
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the presentation of three synchronous extra-adrenal abdominal paragangliomas in an adolescent boy who carries a germline mutation in the SDHB gene are reported. Loss of heterozygosity of this allele is demonstrated by direct sequencing of DNA from two of his tumors, confirming loss of tumor suppressor function in the pathogenesis of these paragangliomas
malfunction
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the frequency of polymorphisms of SDHs, hypoxia-inducible factor type 1 and angiotensin converting enzyme genes is compared between 40 subjects with intolerance to high altitude and a low hypoxic ventilatory response at exercise and 41 subjects without intolerance to high altitude and a high hypoxic ventilatory. No significant association between low or high hypoxic ventilatory response and the allele frequencies for nine single nucleotide polymorphisms in the SDHD and SDHB genes, the ACE insertion/deletion polymorphism and four single nucleotide polymorphisms in the hypoxia-inducible factor type 1 a gene is found. No clear association is found between gene variants involved in oxygen sensing and chemoresponsiveness, although some mutations in the SDHB and SDHD genes deserve further investigations in a larger population
malfunction
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the succinate:ubiquinone oxidoreductase activity of the mitochondrial respiratory complex II is specifically impaired by reactive oxygen species without affecting the second enzymatic activity of this complex as a succinate dehydrogenase. The different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification. Complex II contributes to apoptosis induction only when the SQR activity is inhibited while the SDH activity is still fully functioning,creating an uncoupling phenomenon at the complex II level. The association of an active SDH activity with an inhibited SQR function is not possible, rendering complex II incapable of apoptosis induction and promoting tumourigenesis
physiological function
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the enzyme is involved in electron transfer via the respiratory chain
physiological function
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the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain
physiological function
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the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain
physiological function
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the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview
physiological function
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the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
-
the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
-
the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
-
using the submitochondrial particles from the adult worms and L3 larvae of the parasitic nematode Ascaris suum, it is shown that reactive oxygen species are produced from the flavin adenine dinucleotide-binding site as well as the quinone binding site in the mitochondrial complex II
physiological function
-
using pharmacological and siRNA methodologies it is shown that increased methylation of histone H3 is a general consequence of SDH loss-of-function in cultured mammalian cells and can be reversed by overexpression of the JMJD3 histone demethylase. ChIP analysis reveals that the core promoter of IGFBP7, which encodes a secreted protein upregulated after loss of SDHB, shows decreased occupancy by H3K27me3 (histone 3 methylated on residue K27) in the absence of SDH
physiological function
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succinate:ubiquinone oxidoreductase is part of the mitochondrial respiratory complex II
physiological function
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succinate:quinone reductase serves as the respiratory complex II
physiological function
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overexpression of SdhC and SdhD suppresses 1-(4-chlorophenyl)-benzo-2,5-quinone-induced inhibition of complex II activity, increase in mitochondrial levels of reactive oxygen species, and toxicity
physiological function
deletion of the sdh1 operon does not yield any growth phenotypes on succinate or other nonfermentable carbon sources; presence of the Sdh2 operon is essential for growth. Isoform Sdh2 is the generator of the membrane potential under hypoxia
physiological function
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deletion of the sdh1 operon does not yield any growth phenotypes on succinate or other nonfermentable carbon sources; presence of the Sdh2 operon is essential for growth. Isoform Sdh2 is the generator of the membrane potential under hypoxia
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physiological function
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the enzyme is involved in electron transfer via the respiratory chain
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physiological function
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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succinate:quinone reductase serves as the respiratory complex II
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additional information
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the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
fumarate + menaquinol
succinate + menaquinone
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
fumarate + reduced benzyl viologen
succinate + oxidized benzyl viologen
-
-
-
-
r
fumarate + reduced phenazine methosulfate
succinate + phenazine methosulfate
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enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
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-
r
succinate + 1-methoxy-5-methylphenazinium methyl sulfate
fumarate + ?
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-
-
-
?
succinate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol
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the redox potential of the 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone/2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol couple is 90 mV higher than that of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple
-
-
?
succinate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-1,4-benzohydroquinone
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinol
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
-
-
-
-
r
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + 2,3-dimethyl-1,4-naphthoquinol
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
r
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
?
-
i.e. MTT, in presence of phenazine methosulfate, i.e. PMS
-
-
?
succinate + 2-ethyl-3-methyl-1,4-naphthoquinone
fumarate + 2-ethyl-3-methyl-1,4-naphthoquinol
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol
-
the succinate dehydrogenase C subunit is responsible for ubiquinone binding
-
?
succinate + benzyl viologen
fumarate + reduced benzyl viologen
-
-
-
-
?
succinate + ferricyanide
fumarate + ferrocyanide
-
the assay is based on the reduction of ferricyanide to ferrocyanide by SDH activity and on the coupled capture of ferrocyanide by copper. The granular reaction product (copperferrocyanide) is highly electron opaque and is confined exclusively to the mitochondrial membranes.The use of a chelating agent in the incubating medium prevents the diffusion of the dark spots and guarantees their precise localization at the site of SDH activity
-
-
?
succinate + menadione
fumarate + menadiol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + nitro blue tetrazolium
fumarate + formazan
-
yellow dye
blue dye
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
succinate + oxidized benzyl viologen
fumarate + reduced benzyl viologen
-
-
-
-
r
succinate + oxidized donor
?
-
endogenous SDH activity results in blue diphormazan deposits from the nitroblue tetrazolium reduction through succinate oxidation
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
succinate + oxidized phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
?
succinate + phenazine ethosulfate
fumarate + reduced phenazine ethosulfate
-
-
-
-
?
succinate + phenazine methosulfate
fumarate + ?
-
phenazine methosulfate as direct electron acceptor and 2,6-dichlorophenolindophenol as final acceptor
-
-
?
succinate + ubiquinone-1
fumarate + ubiquinol
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
succinate + ubiquinone-2
fumarate + ubiquinol
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
fumarate + electron donor
succinate + oxidized donor
-
-
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
donor: benzyl viologen
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
main reaction for fumarate reductase, reverse reaction only 1% of fumarate reduction
-
-
?
fumarate + electron donor
succinate + oxidized donor
-
donor: anthrahydroquinonesulfonate
-
-
r
fumarate + reduced acceptor
succinate + acceptor
-
the obligate autotroph requires fumarate reductase activity if it performs CO2 fixation via a reductive citric acid cycle
-
-
r
fumarate + reduced acceptor
succinate + acceptor
-
FrdCAB functions in vivo as both the fumarate reductase and the succinate dehydrogenase, with an apparent energetic cost when catalyzing succinate oxidation
-
-
r
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
fumarate + reduced benzyl viologen
succinate + benzyl viologen
-
-
-
-
?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
-
r
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
-
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
ir
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
ir
succinate + acceptor
fumarate + reduced acceptor
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
Sdh produces only superoxide and no H2O2 upon flavin autoxidation, even at high concentrations of succinate
-
-
?
succinate + acceptor
fumarate + reduced acceptor
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
-
decylubiquinone-mediated reduction of dichlorophenol indophenol
-
-
?
succinate + duroquinone
fumarate + duroquinol
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + duroquinone
fumarate + duroquinol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: dichloroindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
comparison of assay methods
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: methylene blue (oxidized)
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
acceptor: ferricyanide
-
-
r
succinate + menaquinone
fumarate + menaquinol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
in the presence of the artificial electron acceptor phenazine methosulfate and the ubiquinone analogue UQ1
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
succinate-dependent, phenazine methosulfate-mediated malonate-sensitive reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
-
-
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
-
-
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
-
-
-
-
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the succinate dehydrogenase activity of mitochondria in adults and larvae are comparable
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
electron acceptor: menaquinone
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
slow inactivation of the the enzyme in the substrate assay mixture containing different concentrations of substrates, succinate and 2,6-dichloroindophenol, the inactivation rate decreases with increasing concentration of succinate, the inactivation is 2,6-dichloroindophenol concentration independent
-
-
succinate + ubiquinone
fumarate + ubiquinol
-
succinate dehydrogenase restores full activity to electron transport particles or complex II preparations whose succinate dehydrogenases have been selectively destroyed at pH 9.3
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II of the mitochondrial oxidative phosphorylating system
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II is the only membrane bound enzyme of the Krebs cycle, and it feeds electrons into the electron transport chain from the oxidation of succinate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
electrons move from the FAD prosthetic group in SDH on to the two matrix subunits via a series of [Fe-S] redox clusters and possibly also via a heme group to end up at the terminal acceptor ubiquinone residing within the membrane subunits CybL and CybS
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the enzyme does not generate a proton motive force during catalysis and are electroneutral, thus, the quinone reduction reaction must consume cytoplasmic protons which are released stoichiometrically during succinate oxidation. Residues SdhBG227, SdhCD95, and SdhCE101 are located at or near the entrance of a water channel that functions as a proton wire connecting the cytoplasm to the quinone binding site in vivo, while an alternative proton pathway exists in vitro only, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
SDH is a key enzyme that catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Functioning as mitochondrial complex II in the electron transport chain, it transfers electrons extracted from succinate to ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
the enzyme is part of the tricarboxylic acid cycle, it is also a tumor suppressor. Succinate stabilizes and activates hypoxia-inducible factor HIFalpha and reversibly and competitively inhibits HIF-prolyl hydroxylase leading to induction of hypoxia in SDH-deficient cells, 2-oxoglutarate overcomes succinate-mediated inhibition of PHD in vitro, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
determination of quinol:fumarate reductase activity using 2,3-dimethyl-1,4-naphthoquinol
-
r
succinate + ubiquinone
fumarate + ubiquinol
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
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, role of Tyr-89 in the protonation of ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
SDH is an essential component of the electron transport chain and of the tricarboxylic acid cycle in the mitochondrial membrane
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
electrons are transferred from succinate to ubiquinone through the buried prosthetic groups FAD, [2Fe-2S] cluster, [4Fe-4S] cluster [3Fe-4S] cluster and heme, which form an integral part of the complex
-
-
?
additional information
?
-
-
fumarate reductase activity of larval complex II is less than 3% of that of adult enzyme, complex II of adult nematode functions in the reverse direction as a fumarate reductase rather than as a succinate dehydrogenase
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
complex II of adult organism muscle exhibits high fumarate reductase activity and plays a key role in anaerobic electron-transport during adaptation to their microaerobic habitat, in contrast larval complex II shows a much lower fumarate reductase activity than the adult enzyme and functions as succinate dehydrogenase in aerobic respiration
-
-
-
additional information
?
-
-
complex II from mitochondria of the adult parasitic nematode exhibits a high fumarate reductase activity and plays a key role in the anaerobic electron transport observed in these organelles
-
-
-
additional information
?
-
-
enzyme also accetps phenazine methosulfate, reaction of EC 1.3.5.4
-
-
-
additional information
?
-
-
evidence for proton potential dependent catalysis of succinate oxidation by quinone as well as for proton potential generation upon catalysis of fumarate reduction by quinol
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
pathway of electron transfer in complex II
-
-
-
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
-
additional information
?
-
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
-
additional information
?
-
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
reduction of coenzyme Q and analogues, coenzyme Q2 is the most efficient electron acceptor, coenzyme Q10 in substrate quantities when supplemented with Triton X-100 and a lipid extract is about 75% as efficient as coenzyme Q2
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
study of potential dependecy and pH dependency of reaction, tunnel-diopde effect
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
vitamin E analogues bind to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
-
-
-
additional information
?
-
for enzymatic activity the succinate-dependent, phenazine methosulfate-mediated reduction of dichlorophenol indophenol of crude mitochondrial fractions prepared from the wild type and the P211 mutants is measured
-
-
-
additional information
?
-
-
efficiency with different quinones, in decreasing order: phenazine methosulfate, decylubiquinone, duroquinone, menadione, 2,3-dimethyl-1,4-naphthoquinone
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
pathway of electron transfer in complex II
-
-
-
additional information
?
-
-
study of potential dependecy and pH dependency of reaction, tunnel-diopde effect
-
-
-
additional information
?
-
-
model of fumarate reductase electron-transport chain
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
enzyme operates with both natural quinones, ubiquinone and menaquinone, at a single quinone binding site. Residue Lys228 in subunit FrdB provides a strong hydrogen bond to menaquinone and is essential for reactions with both quinone types. There is similar hydrogen bonding of the C1 carbonyl of both MQ and UQ, whereas there is different hydrogen bonding for their C4 carbonyls
-
-
-
additional information
?
-
-
dichlorophenolindophenol only acceptor when used together with phenazine methosulfate, no reaction with ubiquinones, see EC 1.3.5.1 for SDH- and FRD-complex
-
-
-
additional information
?
-
-
approximately 10% to 15% of paragangliomas are caused by mutations in the succinate dehydrogenase genes SDHB, SDHC, or SDHD
-
-
-
additional information
?
-
-
enzyme subunit mutations are involved in the Carney-Stratakis syndrome and in development of gastrointestinal stromal tumors, overview
-
-
-
additional information
?
-
-
germline mutations in the SDHB, SDHC or SDHD genes cause hereditary paraganglioma tumors which show constitutive activation of homeostatic mechanisms induced by oxygen deprivation/hypoxia, overview
-
-
-
additional information
?
-
-
germline mutations of the gene SDHB encoding succinate dehydrogenase subunit B predispose to malignant paraganglioma. Despite an autosomal dominant pattern of inheritance, penetrance of the disease is incomplete and age dependent, overview
-
-
-
additional information
?
-
-
germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
-
-
-
additional information
?
-
-
high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
-
-
-
additional information
?
-
-
inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies, overview
-
-
-
additional information
?
-
-
mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production, overview, complex II defects are involved in ageing and cancers such as hereditary paraganglioma and familial pheochromocytoma, overview
-
-
-
additional information
?
-
-
mutations of the enzyme can cause hereditary paraganglioma and/or pheochromocytoma, overview
-
-
-
additional information
?
-
-
subunit mutations are involved in development of malignant paragangliomas
-
-
-
additional information
?
-
-
succinate dehydrogenase enzyme subunit B gene mutations cause metastatic pheochromocytoma and paraganglioma, distribution of metastases in different tissues in correlation to the enzyme expression, sites of bone involvement, overview
-
-
-
additional information
?
-
-
the Cowden or Cowden-like syndromes are caused by PTEN mutations of the SDH-D gene, encoding the subunit D, the syndromes are associated with breast, thyroid and endometrial neoplasias, overview
-
-
-
additional information
?
-
-
the nuclear genes SDHD and SDHB encode two mitochondrial enzyme complex II subunits and are associated with the development of familial pheochromocytomas and paraganglioma, i.e. the hereditary pheochromocytoma/paraganglioma syndrome, HPPS, and the following metastasis, overview
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
-
additional information
?
-
-
membrane-bound enzyme of the citric acid cycle and the respiratory chain
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
enzyme assay using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide method
-
-
-
additional information
?
-
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, overview
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
succinate dehydrogenase flavoprotein subunit Sdh1p is bound by the mitochondrial FAD transporter, Flx1p, a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae, FLX1p controls SDH activity by regulating the amount of flavinylated Sdh1p, overview
-
-
-
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
additional information
?
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
no activity with 1,4-benzoquinone
-
-
-
additional information
?
-
-
pathway of electron transfer in complex II
-
-
-
additional information
?
-
-
succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate
-
-
-
additional information
?
-
-
fumarate reduction activity is measured by monitoring photometrically the oxidation of dithionite-reduced benzylviologen by fumarate
-
-
-
additional information
?
-
-
succinate oxidation activity is determined using either methylene blue, dichlorophenolindophenol, ferricenium hexafluorophosphate, dimethylnaphthoquinone or as electron acceptor. Strikingly, no succinate oxidation activity is be detected, independent of the electron acceptor
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
fumarate + menaquinol
succinate + menaquinone
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
fumarate + reduced acceptor
succinate + acceptor
-
the obligate autotroph requires fumarate reductase activity if it performs CO2 fixation via a reductive citric acid cycle
-
-
r
fumarate + reduced acceptor
succinate + acceptor
-
FrdCAB functions in vivo as both the fumarate reductase and the succinate dehydrogenase, with an apparent energetic cost when catalyzing succinate oxidation
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
O73937 and O73937 and O73939 and O73940
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
-
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II of the mitochondrial oxidative phosphorylating system
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
complex II is the only membrane bound enzyme of the Krebs cycle, and it feeds electrons into the electron transport chain from the oxidation of succinate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
-
succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol
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succinate + ubiquinone
fumarate + ubiquinol
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succinate + ubiquinone
fumarate + ubiquinol
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SDH is a key enzyme that catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Functioning as mitochondrial complex II in the electron transport chain, it transfers electrons extracted from succinate to ubiquinone
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succinate + ubiquinone
fumarate + ubiquinol
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the enzyme is part of the tricarboxylic acid cycle, it is also a tumor suppressor. Succinate stabilizes and activates hypoxia-inducible factor HIFalpha and reversibly and competitively inhibits HIF-prolyl hydroxylase leading to induction of hypoxia in SDH-deficient cells, 2-oxoglutarate overcomes succinate-mediated inhibition of PHD in vitro, overview
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succinate + ubiquinone
fumarate + ubiquinol
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-
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succinate + ubiquinone
fumarate + ubiquinol
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SDH is an essential component of the electron transport chain and of the tricarboxylic acid cycle in the mitochondrial membrane
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succinate + ubiquinone
fumarate + ubiquinol
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a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
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additional information
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complex II of adult organism muscle exhibits high fumarate reductase activity and plays a key role in anaerobic electron-transport during adaptation to their microaerobic habitat, in contrast larval complex II shows a much lower fumarate reductase activity than the adult enzyme and functions as succinate dehydrogenase in aerobic respiration
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additional information
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complex II from mitochondria of the adult parasitic nematode exhibits a high fumarate reductase activity and plays a key role in the anaerobic electron transport observed in these organelles
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additional information
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the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
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additional information
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succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
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additional information
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succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
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additional information
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vitamin E analogues bind to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
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additional information
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succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
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additional information
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approximately 10% to 15% of paragangliomas are caused by mutations in the succinate dehydrogenase genes SDHB, SDHC, or SDHD
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additional information
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enzyme subunit mutations are involved in the Carney-Stratakis syndrome and in development of gastrointestinal stromal tumors, overview
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additional information
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germline mutations in the SDHB, SDHC or SDHD genes cause hereditary paraganglioma tumors which show constitutive activation of homeostatic mechanisms induced by oxygen deprivation/hypoxia, overview
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additional information
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germline mutations of the gene SDHB encoding succinate dehydrogenase subunit B predispose to malignant paraganglioma. Despite an autosomal dominant pattern of inheritance, penetrance of the disease is incomplete and age dependent, overview
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additional information
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germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
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additional information
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high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
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additional information
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inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies, overview
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additional information
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mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production, overview, complex II defects are involved in ageing and cancers such as hereditary paraganglioma and familial pheochromocytoma, overview
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additional information
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mutations of the enzyme can cause hereditary paraganglioma and/or pheochromocytoma, overview
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additional information
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subunit mutations are involved in development of malignant paragangliomas
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additional information
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succinate dehydrogenase enzyme subunit B gene mutations cause metastatic pheochromocytoma and paraganglioma, distribution of metastases in different tissues in correlation to the enzyme expression, sites of bone involvement, overview
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additional information
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the Cowden or Cowden-like syndromes are caused by PTEN mutations of the SDH-D gene, encoding the subunit D, the syndromes are associated with breast, thyroid and endometrial neoplasias, overview
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additional information
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the nuclear genes SDHD and SDHB encode two mitochondrial enzyme complex II subunits and are associated with the development of familial pheochromocytomas and paraganglioma, i.e. the hereditary pheochromocytoma/paraganglioma syndrome, HPPS, and the following metastasis, overview
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additional information
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the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
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additional information
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membrane-bound enzyme of the citric acid cycle and the respiratory chain
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additional information
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succinate dehydrogenase flavoprotein subunit Sdh1p is bound by the mitochondrial FAD transporter, Flx1p, a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae, FLX1p controls SDH activity by regulating the amount of flavinylated Sdh1p, overview
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additional information
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female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
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additional information
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female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
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additional information
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succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
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 b556
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ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
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heme b562
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the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
quinone
-
with a periplasmically oriented quinone binding site of the enzyme
cytochrome b
-
cytochrome b-558, 3.6 nmol per mg of protein, functions as electron carrier between NADH dehydrogenase and succinate dehydrogenase in the Ascaris NADH-fumarate reductase system
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cytochrome b
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cytochrome b-558, composed of two hydrophobic polypeptides with molecular masses of 17.2 and 12.5 kDa, which correspond to the two small subunits of complex II
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cytochrome b
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cytochrome b-558, is the smallest protein of the complex with MW: 19000, it is a transmembrane protein and anchors succinate dehydrogenase to the cytoplasmic side of the membrane
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cytochrome b
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the isolated two-subunit membrane anchoring protein contains 35 nmol cytochrome b-556 per mg protein
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FAD
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1 mol of covalently bound flavin per 100,000 g of protein; covalently bound to flavoprotein subunit
FAD
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ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
FAD
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flavoprotein, 41 pmol FAD per mg of protein in wild-type strain YPH499, possesses a flavoprotein subunit Sdh1p as part of the catalytic dimer of the tetrameric enzyme
FAD
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proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
FAD
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proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
FAD
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FAD is non-covalently attached to SdhA. The reason for the lack of succinate oxidation activity might be explained by the absence of a covalently bound FAD which seems to be a prerequisite for succinate oxidation activity
FAD
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stoichiometric ratio between covalently bound FAD and the iron-sulfur cluster is 1:1. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
FAD
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FAD of Sdh1 is covalently attached at an active site His residue, 8alpha-N3-histidyl-FAD linkage, involving Arg582, required for enzyme activity. Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit. FAD binding is important to stabilize the Sdh1 conformation enabling association with Sdh2 and the membrane anchor subunits
FAD
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flavinylation of SDH is dependent on SDH1:SDHA F2 interaction requiring the C-terminal tail of SDH1
flavin
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the enzyme complex contains non-extractable flavin. The purified complex contains 4.6 nmol/mg acid non-extractable flavin
flavin
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quantitative determination of content in wild-type and mutant enzymes
heme
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enzyme contains two heme molecules. Presence of protoheme IX, absence of the other heme types. The ratio of protoheme IX to the SQR protomer is 1.5, there are two protoheme IX-binding sites in SQR
heme
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direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
heme
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a single heme b moiety is incorporated into the membrane anchor and only the QP-site is functional
heme
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in a di-heme membrane anchor protein harboring two putative quinone binding sites
heme
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proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
heme
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
heme
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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. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
heme b
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the enzyme contains one hydrophobic subunit (C) with two haem b groups
heme b
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the quinone binding site of succinate dehydrogenase is required for electron transfer to the heme b
iron-sulfur centre
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direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
iron-sulfur centre
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ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
iron-sulfur centre
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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. The purified mQFR complex has two iron-sulfur centers of the ferredoxin type that are paramagnetic in the reduced state, 2Fe-2S and 4Fe-4S, and one iron-sulfur center of the high potential type that is paramagnetic in the oxidized state, 3Fe-4S. Centers 2Fe-2S and 4Fe-4S exhibit a large difference in their redox midpoint potential, center 2Fe-2S is reducible with succinate, whereas the latter one can only be reduced by very low potential reductant such as dithionite
iron-sulfur centre
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enzyme contains the canonical iron-sulfur centers S1, S2, and S3, as well as two B-type hemes. The S3 center has a high reduction potential of +130 mV and is present in two different conformations, one of which presents an EPR signal with g values at 2.035, 2.009, and 2.001. The apparent midpoint reduction potentials of the hemes, +75 and -65 mV at pH 7.5, are higher than those reported for other enzymes. The heme with the lower potential, heme bL, presents a considerable dependence of the reduction potential with pH, i.e. a redox-Bohr effect, having a pKox of 6.5 and a pKred of 8.7. This behavior is consistent with the proposal that in these enzymes menaquinone reduction occurs close to heme bL, near to the periplasmic side of the membrane, and involving dissipation of the proton transmembrane gradient
ubiquinone
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two putative binding sites in the di-heme membrane anchoring protein
ubiquinone
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the residues required for quinone-binding are harbored by SdhD
additional information
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preparations of complex II contain 0.2 mg lipid per mg protein and 7-8 mol of acid-labile sulfide per 100,000 g of protein
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additional information
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the enzyme contains iron-sulfur centers; the iron-sulfur clusters are located in one or both of the hydrophilic subunits, centre 2 in fumarate reductase is a 4Fe-4S cluster
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additional information
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measurement of the redox potentials of the sulfur-centers; the enzyme contains iron-sulfur centers
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additional information
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measurement of the redox potentials of the sulfur-centers; the enzyme contains iron-sulfur centers
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additional information
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analysis of the functional role of the trinuclear cluster S3 in the enzyme by introducing a fourth cysteine residue into the putative ligation motif to that cluster; the enzyme contains iron-sulfur centers
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additional information
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the enzyme contains iron-sulfur centers; the fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit, at least the flavoprotein subunit and the small subunit of cytochrome b of the larval complex II differ from those of adult
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additional information
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the enzyme contains iron-sulfur centers
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additional information
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two hydrophobic subunits (C and D) which bind either one haem b group
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3Fe-4S center
4Fe-4S cluster
Q97W79; Q97W78; Q97W77; Q97W76;
the CCG-domain-containing subunit SdhE (formerly SdhC) contains a [4Fe–4S] cluster in reduced (2+) and oxidized (3+) states. The reduced form of the [4Fe–4S]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
Anions
Ca2+
Fe
Fe-S cluster
Fe-S-clusters
Fe2+
Iron
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
Iron-sulfur cluster
[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 iron–sulfur subunit of succinate dehydrogenase
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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3Fe-4S, bound to Ip subunit; 4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
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3Fe-4S, bound to Ip subunit; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller 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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4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
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 [3Fe–4S]1+,0 cluster
Fe-S-clusters
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magnetic circular dichroism study of Fe-S-clusters S1-S3; 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; 4Fe-4S centre, bound to Fp (Fp: flavoprotein subunit, larger) subunit or bridging between Ip and Fp subunits; types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
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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contains two 2Fe-2S-centers and one 4Fe-4S-center per mol of histidyl flavin
Fe2+
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heme cofactor and [3Fe-4S] cluster, midpoint potentials of wild-type and mutant enzymes, overview
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+
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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+
D2KQI9;
iron sulfur subunit of the succinate dehydrogenase protein complex
Fe2+
-
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
Iron
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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
-
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
-
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
-
Sdh2 subunit contains [2Fe-2S], 4[Fe-4S] and [3Fe-4S] clusters
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 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
-
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one