Single-turnover intermolecular reaction between a Fe(III)-superoxide-Cu(I) cytochrome c oxidase model and exogeneous Tyr244 mimics.
An Fe(III)-superoxide-Cu(I) cytochrome c oxidase model reacts intermolecularly with hindered phenols leading to phenoxyl radicals, as was observed in the enzyme and evidence for the formation of an Fe(IV)-oxo is presented.
Collman
James P
JP
Stanford University, Chemistry Department, Stauffer II, Stanford, CA-94306, USA. jpc@stanford.edu
Decréau
Richard A
RA
Sunderland
Christopher J
CJ
D001665:Binding Sites; D002412:Cations; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D004789:Enzyme Activation; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism; D005609:Free Radicals; D008958:Models, Molecular; D018716:Molecular Mimicry; D009942:Organometallic Compounds / Q000138:chemical synthesis; D010636:Phenols / Q000737:chemistry; D013057:Spectrum Analysis; D013481:Superoxides / Q000737:chemistry* / Q000378:metabolism; D014443:Tyrosine / Q000737:chemistry*
D002412:Cations; D005290:Ferric Compounds; D005609:Free Radicals; D009942:Organometallic Compounds; D010636:Phenols; D013481:Superoxides; D014443:Tyrosine; D003300:Copper; D003576:Electron Transport Complex IV