Pyruvate-ferredoxin oxidoreductase: Difference between revisions

Revision as of 16:11, 22 August 2019

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 are shown as red spheres. .

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

Drag the structure with the mouse to rotate

3D structures of pyruvate-ferredoxin oxidoreductase3D structures of pyruvate-ferredoxin oxidoreductase

22-August-2019

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
6cin – MtPFOR + TDP – Moorella thermoacetica
6cio, 6cip – MtPFOR + TTP derivative
6ciq – MtPFOR + TTP + CoA

ReferencesReferences

↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[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

[1]

[2]

@@ Line 5: / Line 5: @@
 == Structural highlights ==
-The <scene name='49/490113/Cv/6'>active site of PFOR contains thiamine diphosphate and pyruvate</scene><ref>PMID:16472741</ref>. Water molecules are shown as red spheres. <scene name='49/490113/Cv/7'>Mg coordination site</scene>.
+The <scene name='49/490113/Cv/6'>active site of PFOR contains thiamine diphosphate and pyruvate</scene><ref>PMID:16472741</ref>. <scene name='49/490113/Cv/7'>Mg coordination site</scene>. Water molecules are shown as red spheres. <scene name='49/490113/Cv/8'>Fe4S4 cluster interactions</scene>.
 </StructureSection>
 ==3D structures of pyruvate-ferredoxin oxidoreductase==