The enzyme is found in formate-oxidizing CO2-reducing methanogenic archaea such as Methanococcus maripaludis. It consists of a cytoplasmic complex of HdrABC reductase and formate dehydrogenase. Electron pairs donated by formate dehydrogenase are transferred to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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The enzyme appears in viruses and cellular organisms
The enzyme is found in formate-oxidizing CO2-reducing methanogenic archaea such as Methanococcus maripaludis. It consists of a cytoplasmic complex of HdrABC reductase and formate dehydrogenase. Electron pairs donated by formate dehydrogenase are transferred to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
electron flow occurs from formate 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
electron flow occurs from formate 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
the protein complex consists of heterodisulfide reductase, formylmethanofuran dehydrogenase, F420-nonreducing hydrogenase, and formate dehydrogenase. Either H2 or formate can donate electrons to the heterodisulfide-H2 via F420-nonreducing hydrogenase or formate via formate dehydrogenase. When H2 is used as the electron donor for methanogenesis, electrons are transferred to heterodisulfide reductase via F420-nonreducing hydrogenase. Flavin-mediated electron bifurcation at heterodisulfide reductase A then results in reduction of the CoM-S-S-CoB heterodisulfide and a ferredoxin that is used by formylmethanofuran dehydrogenase for the first step in methanogenesis. When hydrogen is limiting or is replaced by formate, formate dehydrogenase is highly expressed and incorporates into the complex. When formate is used as the electron donor for methanogenesis, electrons are transferred to heterodisulfide reductase from formate via formate dehydrogenase
in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Fdh containing complexes show higher activity with formate compared to hydrogen. The non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Fdh containing complexes show higher activity with formate compared to hydrogen. The non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
a methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1
activates HdrDE activity, best at 3 M KCl, about 50% activity at 2 and 4 M KCl. Formate oxidation by FdhGHI is slightly lower with 2 M KCl instead of NaCl
the FBEB specific activity is slightly reduced when 1.6 M phosphate is replaced with 1.5 M phosphate buffer and 100 mM MOPS, although a similar activity is observed in 1.5 M ammonium sulfate and 100 mM MOPS. The FBEB specific activity is significantly reduced in 1.6 M MOPS
high concentrations of phosphate buffer are required for optimal FBEB activities in vitro, which because they promote hydrophobic protein-protein interactions between the inserted Fd domain on HdrA and Fd
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 7.5, temperature not specified in the publication, at 2 M KCl
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 8.5, temperature not specified in the publication, at 2 M KCl
FdhGHI activity on formate with methyl viologen as artificial electron acceptor, membrane fraction, pH 9.5, temperature not specified in the publication, at 2 M NaCl
thiol production from the reduction in CoM-S-SCoB with formate as electron donor is also measured with a rate of 369 nmol/mg/min under an N2 atmosphere
and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a poly-His-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a poly-His-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
Methanonatronarchaeum thermophilum strain AMET1 is able to grow on all tested substrates (methanol, trimethylamine (TMA), dimethylamine (DMA), monomethylamine (MMA)) in combination with formate or molecular hydrogen. Growth parameter during methanogenesis from methylated C1-compounds and formate, overview
Methanonatronarchaeum thermophilum strain AMET1 is able to grow on all tested substrates (methanol, trimethylamine (TMA), dimethylamine (DMA), monomethylamine (MMA)) in combination with formate or molecular hydrogen. Growth parameter during methanogenesis from methylated C1-compounds and formate, overview
the catalytic subunit of heterodisulfide reductase (HdrD) is located at the cytoplasmic side of the cytoplasmic membrane. The oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI)
the catalytic subunit of heterodisulfide reductase (HdrD) is located at the cytoplasmic side of the cytoplasmic membrane. The oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI)
heterodisulfide reductase plays a central role in the methanogenesis cycle of Methanococcus maripaludis. In methanogens without cytochromes, the initial endergonic reduction of CO2 to formylmethanofuran with H2-derived electrons is coupled to the exergonic reduction of a heterodisulfide of coenzymes B and M by flavin-based electron bifurcation (FBEB). Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for FBEB using hydrogen and formate. In Methanococcus maripaludis, FBEB is performed by a heterodisulfide reductase (Hdr) enzyme complex that involves hydrogenase (Vhu), although formate dehydrogenase (Fdh) has been proposed as an alternative to Vhu
the oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI), whereas the oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC). Based on this, the electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system, overview. Three energy-conserving, membrane-bound electron transport systems are known in methanogens: (a) H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.5), (b) coenzyme F420H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.4), and (c) reduced ferredoxin:CoM-S-S-CoB oxidoreductase (EC 1.8.7.3)
heterodisulfide reductase plays a central role in the methanogenesis cycle of Methanococcus maripaludis. In methanogens without cytochromes, the initial endergonic reduction of CO2 to formylmethanofuran with H2-derived electrons is coupled to the exergonic reduction of a heterodisulfide of coenzymes B and M by flavin-based electron bifurcation (FBEB). Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for FBEB using hydrogen and formate. In Methanococcus maripaludis, FBEB is performed by a heterodisulfide reductase (Hdr) enzyme complex that involves hydrogenase (Vhu), although formate dehydrogenase (Fdh) has been proposed as an alternative to Vhu
the oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI), whereas the oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC). Based on this, the electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system, overview. Three energy-conserving, membrane-bound electron transport systems are known in methanogens: (a) H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.5), (b) coenzyme F420H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.4), and (c) reduced ferredoxin:CoM-S-S-CoB oxidoreductase (EC 1.8.7.3)
the energy conservation of Methanonatronarchaeum thermophilum is dependent on a respiratory chain consisting of a hydrogenase (VhoGAC, EC 1.8.98.5), a formate dehydrogenase (FdhGHI, EC 1.8.98.6), and a heterodisulfide reductase (HdrDE) that are well adapted to the harsh physicochemical conditions in the natural habitat. Methanogen Methanonatronarchaeum thermophilum is an extremely haloalkaliphilic and moderately thermophilic archaeon. A methanophenazine-like cofactor might function as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase. A methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1. The electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system
the energy conservation of Methanonatronarchaeum thermophilum is dependent on a respiratory chain consisting of a hydrogenase (VhoGAC, EC 1.8.98.5), a formate dehydrogenase (FdhGHI, EC 1.8.98.6), and a heterodisulfide reductase (HdrDE) that are well adapted to the harsh physicochemical conditions in the natural habitat. Methanogen Methanonatronarchaeum thermophilum is an extremely haloalkaliphilic and moderately thermophilic archaeon. A methanophenazine-like cofactor might function as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase. A methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1. The electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system
when grown on formate as its sole electron donor, Methanococcus maripaludis assembles three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex). Protein-protein interaction/docking analysis and modeling, usage of the crystal structure of the analogous MvhHdr complex from Methanothermococcus thermolithotrophicus (PDB ID 5ODC) as template, enzyme complex structures comparisons, overview
when grown on formate as its sole electron donor, Methanococcus maripaludis assembles three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex). Protein-protein interaction/docking analysis and modeling, usage of the crystal structure of the analogous MvhHdr complex from Methanothermococcus thermolithotrophicus (PDB ID 5ODC) as template, enzyme complex structures comparisons, overview
three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex)
three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex)
Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for flavin-based electron bifurcation using hydrogen and formate