Pyruvate-ferredoxin oxidoreductase: Difference between revisions

Latest revision as of 11:23, 4 October 2023

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. . Each Fe atom interacts with S atom from cysteine.

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

04-October-2023

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
7plm – DaPFOR + TPP – Cryo EM
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

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@@ Line 1: / Line 1: @@
-<Structure load='2c3o' size='400' frame='true' align='right' caption=' Pyruvate-ferredoxin oxidoredoxin with Fe4S4 cluster complex with thiamin diphosphate and pyruvate [[2c3o]]' scene= />
+<StructureSection load='2c3o' size='350' side='right' scene='49/490113/Cv/1' caption='Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamine diphosphate and pyruvate [[2c3o]]'>
-<!--
+== Function ==
-Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+'''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>).
-Or use the four-green-boxes-button to insert scrollable text adjacent
-to a Jmol applet. Check out the other buttons as well!
--->
-'''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).
+== Structural highlights ==
+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>. Each Fe atom interacts with S atom from cysteine.
+</StructureSection>
 ==3D structures of pyruvate-ferredoxin oxidoreductase==
+{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 [[1b0p]], [[2c3m]] – DaPFOR + TDP – ''Desulfovibrio africanus''<br />
 [[2pda]], [[2c3o]], [[2c42]] - DaPFOR + pyruvate + TDP<br />
-[[1kek]], [[2c3y]] - DaPFOR + CO2 + acetyl-TDP<br />
+[[1kek]], [[2c3y]], [[2uza]] - DaPFOR + CO2 + acetyl-TDP<br />
 [[2c3p]] - DaPFOR + TDP derivative<br />
 [[2c3u]] - DaPFOR + pyruvate + TDP derivative<br />
-[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''
+[[7plm]] – DaPFOR + TPP – Cryo EM<br />
+[[2raa]] - PFOR γ subunit - ''Thermotoga maritima''<br />
+[[6cin]] – MtPFOR + TDP – ''Moorella thermoacetica''<br />
+[[6cio]], [[6cip]] – MtPFOR + TTP derivative <br />
+[[6ciq]] – MtPFOR + TTP + CoA <br />
+== References ==
+<references/>
 [[Category:Topic Page]]