Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme?
The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evidence that carbon monoxide and cyanide bind synergically to the oxidised and semireduced states of the isolated cofactor, states which are unreactive to carbon monoxide alone.
Pickett
Christopher J
CJ
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK. chris.pickett@bbsrc.ac.uk
Vincent
Kylie A
KA
Ibrahim
Saad K
SK
Gormal
Carol A
CA
Smith
Barry E
BE
Fairhurst
Shirley A
SA
Best
Stephen P
SP
D002248:Carbon Monoxide / Q000378:metabolism*; D003486:Cyanides / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D007711:Klebsiella pneumoniae / Q000201:enzymology; D008958:Models, Molecular; D008983:Molybdoferredoxin / Q000737:chemistry / Q000378:metabolism*; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
D003486:Cyanides; D008983:Molybdoferredoxin; D002248:Carbon Monoxide; D009591:Nitrogenase