Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase.
The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have shed more light on its thiamin-based mechanism of catalysis. Different approaches have been used to study the interaction between the enzyme and ferredoxin, its redox partner.
Charon
M H
MH
Laboratoire de Cristallographie et de Cristallogenèse des Protéines, Institut de Biologie Structurale J-P Ebel (CEA, CNRS), Grenoble, 38027, France. charon@ibs.fr
Volbeda
A
A
Chabriere
E
E
Pieulle
L
L
Fontecilla-Camps
J C
JC
D004579:Electron Transport; D007658:Ketone Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D050743:Pyruvate Synthase; D019289:Pyruvic Acid / Q000378:metabolism; D013835:Thiamine Pyrophosphate / Q000378:metabolism
D019289:Pyruvic Acid; D007658:Ketone Oxidoreductases; D050743:Pyruvate Synthase; D013835:Thiamine Pyrophosphate