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Literature summary for 1.8.98.5 extracted from

  • Appel, L.; Willistein, M.; Dahl, C.; Ermler, U.; Boll, M.
    Functional diversity of prokaryotic HdrA(BC) modules Role in flavin-based electron bifurcation processes and beyond (2021), Biochim. Biophys. Acta, 1862, 148379 .
    View publication on PubMed
Search for more literature for 1.8.98.5

Activating Compound

Activating Compound Comment Organism Structure
CoM-S-S-CoB disulfide reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide Methanothermobacter wolfeii
CoM-S-S-CoB disulfide reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide Methanothermobacter marburgensis
CoM-S-S-CoB disulfide reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide Methanothermococcus thermolithotrophicus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of the heterododecameric enzyme Methanothermococcus thermolithotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter wolfeii
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermococcus thermolithotrophicus
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis Marburg
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis ATCC BAA-927
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis NBRC 100331
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis JCM 14651
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis DSM 2133
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanothermobacter marburgensis OCM 82
-
 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis ATCC BAA-927 Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis DSM 2133 Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis JCM 14651 Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis Marburg Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis NBRC 100331 Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter marburgensis OCM 82 Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
-
Methanothermobacter wolfeii
-
-
-
Methanothermococcus thermolithotrophicus A0A2D0TCB9 AND A0A2D0TCB4 AND A0A2D0TC97 AND A0A2D0TCA6 AND A0A2D0TC99 AND A0A2D0TC98 genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD
-

Reaction

Reaction Comment Organism Reaction ID
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD Methanothermobacter wolfeii
a
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD Methanothermobacter marburgensis
a
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD Methanothermococcus thermolithotrophicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter wolfeii 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermococcus thermolithotrophicus 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor Methanothermobacter wolfeii 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor Methanothermococcus thermolithotrophicus 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis Marburg 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis Marburg 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis ATCC BAA-927 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis ATCC BAA-927 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis NBRC 100331 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis NBRC 100331 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis JCM 14651 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis JCM 14651 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis DSM 2133 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis DSM 2133 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanothermobacter marburgensis OCM 82 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor Methanothermobacter marburgensis OCM 82 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?

Subunits

Subunits Comment Organism
heterododecamer (MvhAGD-HdrABC)2 , 1 * 72000, HdrA, + 1 * 33000, HdrB, + 1 * 21000, HdrC, + 1 * 53000, MvhA, + 1 * 34000, MvhG, + 1 * 16000, MvhD, SDS-PAGE Methanothermococcus thermolithotrophicus
More domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA (72 kDa), HdrB (33 kDa) and HdrC (21 kDa) and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA (53 kDa), MvhG (34 kDa) and MvhD (16 kDa). Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. 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. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex Methanothermococcus thermolithotrophicus
More domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. 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. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex Methanothermobacter wolfeii
More domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. 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. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex Methanothermobacter marburgensis

Synonyms

Synonyms Comment Organism
HdrABC-MvhAGD
-
 Methanothermobacter wolfeii
HdrABC-MvhAGD
-
 Methanothermobacter marburgensis
HdrABC-MvhAGD
-
 Methanothermococcus thermolithotrophicus

Cofactor

Cofactor Comment Organism Structure
FAD electron-bifurcating FAD in HdrA Methanothermobacter wolfeii
FAD electron-bifurcating FAD in HdrA Methanothermobacter marburgensis
FAD electron-bifurcating FAD in HdrA Methanothermococcus thermolithotrophicus
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 Methanothermobacter wolfeii
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 Methanothermobacter marburgensis
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 Methanothermococcus thermolithotrophicus
Ferredoxin standard HdrC-like components consist of a Fd-like domain Methanothermobacter wolfeii
Ferredoxin standard HdrC-like components consist of a Fd-like domain Methanothermobacter marburgensis
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 Methanothermococcus thermolithotrophicus
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 Methanothermobacter wolfeii
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 Methanothermobacter marburgensis
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 Methanothermococcus thermolithotrophicus
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 Methanothermococcus thermolithotrophicus

General Information

General Information Comment Organism
evolution general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. 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. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD 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 Methanothermobacter wolfeii
evolution general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. 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. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD 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 Methanothermobacter marburgensis
evolution general architecture and occurrence of HdrA(BC)-containing complexes, X-ray structure of the MvhAGD-HdrABC complex of Methanothermococcus thermolithotrophicus, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. 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. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD 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 Methanothermococcus thermolithotrophicus
additional information the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). 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. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview Methanothermobacter wolfeii
additional information the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). 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. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview Methanothermobacter marburgensis
additional information the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). 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. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview Methanothermococcus thermolithotrophicus
physiological function the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview Methanothermobacter wolfeii
physiological function the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview Methanothermobacter marburgensis
physiological function the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview Methanothermococcus thermolithotrophicus