Pyruvate-ferredoxin oxidoreductase

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Function

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[1]. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe4S4).

Structural highlights

The [2]. . Water molecules shown as red spheres.

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

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3D structures of pyruvate-ferredoxin oxidoreductase3D 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


ReferencesReferences

  1. Furdui C, Ragsdale SW. The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem. 2000 Sep 15;275(37):28494-9. PMID:10878009 doi:http://dx.doi.org/10.1074/jbc.M003291200
  2. Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC. Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate. Structure. 2006 Feb;14(2):217-24. PMID:16472741 doi:10.1016/j.str.2005.10.013

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Michal Harel, Alexander Berchansky