Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate.
Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum reversibly catalyzes the oxidation of CO to CO(2) at the active site C-cluster. In this article, the reduction of CO(2) to formate is reported as a slow side reaction catalyzed by both Ni-containing CODH and Ni-deficient CODH. Recently, the structures of R. rubrum CODH and its active site NiFeS cluster (the C-cluster) have been solved. The data in this manuscript describe the formate-producing capability of CODH with or without Ni in the active site.
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, 53706-1544, USA.
Jongyun
J
Heo
Lars
L
Skjeldal
Christopher R
CR
Staples
P W
PW
Ludden
D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D003486:Cyanides / Q000378:metabolism / Q000494:pharmacology; D005561:Formates / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D009532:Nickel / Q000378:metabolism; D010084:Oxidation-Reduction; D011522:Protons; D012247:Rhodospirillum rubrum / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development; D013431:Sulfates / Q000378:metabolism
D003486:Cyanides; D005561:Formates; D009097:Multienzyme Complexes; D011522:Protons; D013431:Sulfates; D009532:Nickel; D007501:Iron; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase