Pyruvate-ferredoxin oxidoreductase
From Proteopedia
(Difference between revisions)
| 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= /> | ||
| + | |||
<!-- | <!-- | ||
Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page. | Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page. | ||
Revision as of 10:51, 17 April 2012
|
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
1b0p, 2c3m – DaPFOR + TDP – Desulfovibrio africanus
2pda, 2c3o, 2c42 - DaPFOR + pyruvate + TDP
1kek, 2c3y - DaPFOR + CO2 + acetyl-TDP
2c3p - DaPFOR + TDP derivative
2c3u - DaPFOR + pyruvate + TDP derivative
2raa - PFOR γ subunit - Thermotoga maritima
