Binding of CO to structural models of the bimetallic subunit at the A-cluster of acetyl coenzyme A synthase/CO dehydrogenase.
Trinuclear Ni-Cu-Ni and Ni-Ni-Ni complexes derived from an Ni(ii)-dicarboxamido-dithiolato metallosynthon exhibit redox behavior and CO binding properties similar to those of the A-cluster in acetyl coenzyme A synthase/CO dehydrogenase (ACS/CODH).
Harrop
Todd C
TC
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Olmstead
Marilyn M
MM
Mascharak
Pradip K
PK
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D002248:Carbon Monoxide / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry*; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000378:metabolism; D009532:Nickel / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction
D009097:Multienzyme Complexes; D003300:Copper; D009532:Nickel; D002248:Carbon Monoxide; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase