Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.98.6 extracted from

  • Steiniger, F.; Sorokin, D.; Deppenmeier, U.
    Process of energy conservation in the extremely haloalkaliphilic methyl-reducing methanogen Methanonatronarchaeum thermophilum (2022), FEBS J., 289, 549-563 .
    View publication on PubMed

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 [Āµmol/min/mg] Specific Activity Maximum [Āµmol/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