Molybdenum(V) sites in xanthine oxidase and relevant analog complexes: comparison of molybdenum-95 and sulfur-33 hyperfine coupling

super(95)Mo (I = 5/2) hyperfine matrices have been defined from multifrequency (2-4 and 9 GHz) electron spin resonance spectra of the Rapid Type 1, Rapid Type 2, and Slow centers of milk xanthine oxidase. The present work suggests a specific mechanism: reduction of the Mo super(VI)OS resting form to...

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Veröffentlicht in:	Journal of the American Chemical Society 1991-08, Vol.113 (18), p.6803-6812
Hauptverfasser:	Wilson, Graham L, Greenwood, Richard J, Pilbrow, John R, Spence, Jack T, Wedd, Anthony G
Format:	Artikel
Sprache:	eng
Schlagworte:	Atomic and molecular physics binding characterization chemical properties Electron resonance and relaxation Exact sciences and technology Molecular properties and interactions with photons molybdenum V Physics sites xanthine oxidase
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Zusammenfassung:	super(95)Mo (I = 5/2) hyperfine matrices have been defined from multifrequency (2-4 and 9 GHz) electron spin resonance spectra of the Rapid Type 1, Rapid Type 2, and Slow centers of milk xanthine oxidase. The present work suggests a specific mechanism: reduction of the Mo super(VI)OS resting form to Mo super(V) or Mo super(IV) causes occupation of a highly covalent MoS pi -antibonding orbital with a consequence increase in the basicity of the thio ligand.
ISSN:	0002-7863 1520-5126
DOI:	10.1021/ja00018a014