Physics Commons^™

Evidence Favoring Molybdenum−Carbon Bond Formation In Xanthine Oxidase Action: 17O- And 13C-Endor And Kinetic Studies, Barry D. Howes, Robert C. Bray, Raymond L. Richards, Nigel A. Turner, Brian Bennett, David J. Lowe

Physics Faculty Research and Publications

The reaction mechanism of the molybdoenzyme xanthine oxidase has been further investigated by ¹³C and ¹⁷O ENDOR of molybdenum(V) species and by kinetic studies of exchange of oxygen isotopes. Three EPR signal-giving species were studied:  (i) Very Rapid, a transient intermediate in substrate turnover, (ii) Inhibited, the product of an inhibitory side reaction with aldehyde substrates, and (iii) Alloxanthine, a species formed by reaction of reduced enzyme with the inhibitor, alloxanthine. The Very Rapid signal was developed either with [8-¹³C]xanthine or with 2-oxo-6-methylpurine using enzyme equilibrated with [¹⁷O]H₂O. The Inhibited signal was …