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Literature summary for 1.8.98.6 extracted from
- Process of energy conservation in the extremely haloalkaliphilic methyl-reducing methanogen Methanonatronarchaeum thermophilum (2022), FEBS J., 289, 549-563 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition of HdrDE and FdhGHI by diphenyleneiodonium chloride | Methanonatronarchaeum thermophilum | |
| NaCl | - |
Methanonatronarchaeum thermophilum |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | 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) | Methanonatronarchaeum thermophilum | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| KCl | 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 | Methanonatronarchaeum thermophilum | |
| additional information | at pH 7.5, the specific activity of HdrDE with 2 M potassium chloride is about 40% higher than with 2 M sodium chloride | Methanonatronarchaeum thermophilum | |
| NaCl | activates FdhGHI activity, best at 2 M, formate oxidation is slightly lower with 2 M KCl instead of NaCl | Methanonatronarchaeum thermophilum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | Methanonatronarchaeum thermophilum | - |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | Methanonatronarchaeum thermophilum AMET1 | - |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanonatronarchaeum thermophilum | A0A1Y3GAE7 | CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake | - |
| Methanonatronarchaeum thermophilum AMET1 | A0A1Y3GAE7 | CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | 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 | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
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 | Methanonatronarchaeum thermophilum |
| 3.3 | - |
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 | Methanonatronarchaeum thermophilum |
| 5.9 | - |
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 | Methanonatronarchaeum thermophilum |
| 10.7 | - |
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 | Methanonatronarchaeum thermophilum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
Methanonatronarchaeum thermophilum | 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | 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 | Methanonatronarchaeum thermophilum | 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | - |
Methanonatronarchaeum thermophilum AMET1 | 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
| 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB | 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 | Methanonatronarchaeum thermophilum AMET1 | 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FdhGHI | - |
Methanonatronarchaeum thermophilum |
| formate: CoMS-S-CoB oxidoreductase | - |
Methanonatronarchaeum thermophilum |
| HdrDE | - |
Methanonatronarchaeum thermophilum |
| HdrDE-FdhGHI | - |
Methanonatronarchaeum thermophilum |
| heterodisulfide reductase | - |
Methanonatronarchaeum thermophilum |
| More | see also EC 1.8.98.5 | Methanonatronarchaeum thermophilum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
HdrDE activity | Methanonatronarchaeum thermophilum |
| 9.5 | - |
VhoGAC activity | Methanonatronarchaeum thermophilum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 10.5 | enzyme activity range, profile overview | Methanonatronarchaeum thermophilum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Ferredoxin | - |
Methanonatronarchaeum thermophilum | |
| additional information | a methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1 | Methanonatronarchaeum thermophilum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | 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) | Methanonatronarchaeum thermophilum |
| physiological function | 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 | Methanonatronarchaeum thermophilum |
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