Pyruvate-ferredoxin oxidoreductase

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<Structure load='2c3o' size='400' frame='true' align='right' caption=' Pyruvate-ferredoxin oxidoredoxin with Fe4S4 cluster complex with thiamin diphosphate and pyruvate [[2c3o]]' scene= />
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<Structure load='2c3o' size='400' frame='true' align='right' caption=' Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamin diphosphate and pyruvate [[2c3o]]' scene= />
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Revision as of 09:46, 13 November 2012

Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamin diphosphate and pyruvate 2c3o

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Pyruvate-ferredoxin oxidoreductase (PFOR) is an enzyme of the fermentation cycle which catalyzes the oxidative decarboxylation of pyruvate to acetyl CoA and CO2. This reaction provides the electron source for the reduction of ferredoxin. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe4S4).

3D structures of pyruvate-ferredoxin oxidoreductase

Update June 2012

1b0p, 2c3m – DaPFOR + TDP – Desulfovibrio africanus
2pda, 2c3o, 2c42 - DaPFOR + pyruvate + TDP
1kek, 2c3y, 2uza - DaPFOR + CO2 + acetyl-TDP
2c3p - DaPFOR + TDP derivative
2c3u - DaPFOR + pyruvate + TDP derivative
2raa - PFOR γ subunit - Thermotoga maritima

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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