Pyruvate-ferredoxin oxidoreductase

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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= />
<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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== Function ==
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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 CO<sub>2</sub>. This reaction provides the electron source for the reduction of ferredoxin<ref>PMID:10878009</ref>. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe<sub>4</sub>S<sub>4</sub>).
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== Structural highlights ==
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The active site of PFOR contains thiamine diphosphate and pyruvate<ref>PMID:16472741</ref>.
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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).
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==3D structures of pyruvate-ferredoxin oxidoreductase==
==3D structures of pyruvate-ferredoxin oxidoreductase==
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[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''
[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:21, 2 August 2016

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

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Contents

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 active site of PFOR contains thiamine diphosphate and pyruvate[2].

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


References

  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

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