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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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
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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
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
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
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
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-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
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
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
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
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-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
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
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
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
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
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-
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
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
additional information
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
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coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
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coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
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coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
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H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
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H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
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reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
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reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
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additional information
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Methanobacterium thermoautotrophicus
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no activity with coenzyme F420
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additional information
?
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Methanobacterium thermoautotrophicus DSM 2133
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no activity with coenzyme F420
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additional information
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
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the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
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additional information
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the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
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additional information
?
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
?
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heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
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-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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-
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?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
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-
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-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
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-
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?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
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?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.8.98.5 H2:CoB-CoM heterodisulfide,ferredoxin reductase
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