1.8.98.5: H2:CoB-CoM heterodisulfide,ferredoxin reductase
This is an abbreviated version!
For detailed information about H2:CoB-CoM heterodisulfide,ferredoxin reductase, go to the full flat file.
Word Map on EC 1.8.98.5
-
1.8.98.5
-
methanococcus
-
methanogenic
-
hydrogenases
-
archaea
-
nickel
-
epr
-
voltae
-
sulfur
-
methanosarcina
-
energy-conserving
-
ni
-
hyperfine
-
methanobacterium
-
selenocysteine
-
f420-reducing
-
fad
-
heterolytic
-
methane
-
selenium-containing
-
barkeri
-
illumination
-
selenium
-
thermoautotrophicum
-
com-s-s-cob
-
methanothermobacter
-
hydrogenotrophic
-
non-heme
-
marburgensis
-
acid-labile
- 1.8.98.5
- methanococcus
-
methanogenic
- hydrogenases
- archaea
- nickel
- epr
- voltae
- sulfur
- methanosarcina
-
energy-conserving
- ni
-
hyperfine
-
methanobacterium
- selenocysteine
-
f420-reducing
- fad
-
heterolytic
- methane
-
selenium-containing
- barkeri
- illumination
- selenium
- thermoautotrophicum
- com-s-s-cob
-
methanothermobacter
-
hydrogenotrophic
-
non-heme
- marburgensis
-
acid-labile
Reaction
2 reduced ferredoxin [iron-sulfur] cluster + + + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster +
Synonyms
CoB-CoM heterodisulfide reductase, F420-non-reducing hydrogenase, H2-driven FBEB, H2: CoM-S-S-CoB oxidoreductase, H2: heterodisulfide oxidoreductase complex, HdrA, hdrA1B1C1, HdrABC, HdrABC-MvhAGD, HdrB, HdrC, HdrDE, HdrDE-VhoGAC, heterodisulfide reductase, heterodisulfide reductase complex, hydrogenase, More, Mvh, MvhA, MvhADG, MvhADG/HdrABC, MvhD, MvhG, VhoGAC, Vhu
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.8.98.5 - H2:CoB-CoM heterodisulfide,ferredoxin reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
FAD
electron-bifurcating FAD in HdrA
FAD
electron-bifurcating FAD in HdrA
FAD
-
the bifurcating FAD of HdrA sequentially accepts two electrons from the [2Fe-2S] cluster that contrasts with other characterized FBEB enzymes for which a hydride is donated to FAD
-
two [4Fe-4S] clusters of the inserted ferredoxin (Fd) domain
Fe-S center
-
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Fe-S center
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Fe-S center
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Ferredoxin
-
standard HdrC-like components consist of a Fd-like domain
-
Ferredoxin
standard HdrC-like components consist of a Fd-like domain
-
Ferredoxin
standard HdrC-like components consist of a Fd-like domain. The TrxR domain is flanked by attached N- and C-terminal domains and an inserted Fd domain hosting one, two and again two [4Fe-4S] clusters, respectively. The low-potential acceptor Fd was not found in the complex, but electron transfer to it most possibly involves the [4Fe-4S] cluster of the Fd domain in HdrA
-
a methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1
-
additional information
-
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
the FAD binding site is encapsulated from bulk solvent preventing binding of hydride donors such as NADH or F420H2. The high-potential branch from FAD to the active-site non-cubane [4Fe-4S] clusters in HdrB proceeds via [4Fe-4S] clusters bound to the HdrBC subunits. The non-cubane clusters can be described as fused [3Fe-4S]/[2Fe-2S] subclusters, sharing one iron and one sulfur
-