Transient FTIR spectroelectrochemical and stopped-flow detection of a mixed valence (Fe(I)-Fe(II)) bridging carbonyl intermediate with structural elements and spectroscopic characteristics of the di-iron sub-site of all-iron hydrogenase.
Iron(I) in biology?: one-electron oxidation of an (Fe(I)-Fe(I)) carbonyl cyanide precursor bearing a proximal thioether group leads to an (Fe(I)-Fe(II)) bridging carbonyl transient with spectral features similar to the di-iron sub-site of the CO inhibited paramagnetic centre of all-iron hydrogenase.
Department of Biological Chemistry, John Innes Centre, Norwich, UK NR4 7UH.
Mathieu
M
Razavet
Stacey J
SJ
Borg
Simon J
SJ
George
Stephen P
SP
Best
Shirley A
SA
Fairhurst
Christopher J
CJ
Pickett
D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D004563:Electrochemistry; D006864:Hydrogenase / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry; D015394:Molecular Structure; D009570:Nitriles / Q000737:chemistry; D010084:Oxidation-Reduction; D017550:Spectroscopy, Fourier Transform Infrared / Q000295:instrumentation / Q000379:methods
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D008024:Ligands; D008667:Metalloproteins; D009570:Nitriles; C100076:mesoxalonitrile; C118830:iron hydrogenase; D006864:Hydrogenase