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Literature summary for 1.8.7.3 extracted from

  • Kroeninger, L.; Steiniger, F.; Berger, S.; Kraus, S.; Welte, C.U.; Deppenmeier, U.
    Energy conservation in the gut microbe Methanomassiliicoccus luminyensis is based on membrane-bound ferredoxin oxidation coupled to heterodisulfide reduction (2019), FEBS J., 286, 3831-3843 .
    View publication on PubMed
Search for more literature for 1.8.7.3

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Methanomassiliicoccus luminyensis 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanomassiliicoccus luminyensis
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 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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 ?

Organism

Organism UniProt Comment Textmining
Methanomassiliicoccus luminyensis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
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 Methanomassiliicoccus luminyensis 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
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 ?
additional information thiols are only produced when membranes of Methanomassiliicoccus luminyensis, HdrD, Fd, and IOR are present. In the absence of Fd, HdrD, or washed membranes, thiol formation is very low indicating that all above-mentioned components are necessary for an effective electron transfer from Fdred to CoM-S-S-CoB. Fd:heterodisulfide reductase activity is measured by the oxidation of Fdred as the initial reaction and thiol formation by CoM-S-S-CoB reduction as a final reaction of the proposed electron transport chain. At least one membrane-bound enzyme is needed for electron transport Methanomassiliicoccus luminyensis ?
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Synonyms

Synonyms Comment Organism
ferredoxin:heterodisulfide oxidoreductase
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 Methanomassiliicoccus luminyensis
HdrD
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 Methanomassiliicoccus luminyensis
heterodisulfide reductase
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 Methanomassiliicoccus luminyensis

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
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 Methanomassiliicoccus luminyensis

General Information

General Information Comment Organism
evolution the energy-conserving system in Methanomassiliicoccus luminyensis is unique, and the enzymes involved in this process are not found in this combination in members of the other methanogenic orders. The composition of the enzymes involved in ion translocation across the cytoplasmic membrane is different from all other methanogenic archaea Methanomassiliicoccus luminyensis
metabolism the process of methanogenesis in Methanomassiliicoccus luminyensis involves the transfer of methyl group from methanol or methylamines to 2-mercaptoethanesulfonate (HSCoM). The resulting methyl-S-CoM is reduced to methane by the methyl-CoM reductase which uses 7-mercaptoheptanoylthreonine phosphate (HS-CoB) as a reductant and forms the heterodisulfide (CoM-S-SCoB). The membrane-bound electron transport is based on the headless Fpo complex, which accepts electrons from Fdred and channels these electrons to the heterodisulfide reductase HdrD. And HdrD reduces the final electron acceptor the heterodisulfide (CoB-S-S-CoM) Methanomassiliicoccus luminyensis
physiological function energy conservation in the gut microbe Methanomassiliicoccus luminyensis is based on membrane-bound ferredoxin oxidation coupled to heterodisulfide reduction. Energy transduction is dependent on a membrane-bound ferredoxin:heterodisulfide oxidoreductase composed of reduced ferredoxin as an electron donor, at least one protein in the membrane fraction and the heterodisulfide reductase HdrD, which reduces the electron acceptor CoMS-S-CoB. Electron transfer of this respiratory chain proceeds with a rate of 145 nmol reduced heterodisulfide per min/mg membrane protein. Only protons are used as coupling ions for the generation of the electrochemical ion gradient. The membrane-bound F420H2:phenazine oxidoreductase complex (without the electron input module FpoF) probably catalyzes the oxidation of reduced ferredoxin and potentially acted as primary proton pump in this electron transport system Methanomassiliicoccus luminyensis