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Articles 151 - 152 of 152
Full-Text Articles in Physical Sciences and Mathematics
Epr Studies On The Mono- And Dicobalt(Ii)-Substituted Forms Of The Aminopeptidase From Aeromonas Proteolytica. Insight Into The Catalytic Mechanism Of Dinuclear Hydrolases, Brian Bennett, Richard C. Holz
Epr Studies On The Mono- And Dicobalt(Ii)-Substituted Forms Of The Aminopeptidase From Aeromonas Proteolytica. Insight Into The Catalytic Mechanism Of Dinuclear Hydrolases, Brian Bennett, Richard C. Holz
Physics Faculty Research and Publications
The structure and function of the prototypical dinuclear hydrolase, namely, the aminopeptidase from Aeromonas proteolytica (AAP), was probed by EPR spectroscopy of the mono- and dicobalt(II)-substituted derivatives. A new systematic protocol for the interpretation of Co(II) EPR spectra is described and the S = 3/2 spin states of the Co(II)-substituted forms of the enzyme have been characterized. This protocol allows the simulation of line shape using theoretically allowed geff values corresponding to an isotropic greal value. In addition, the gross distortion of EPR spectra of high-spin S = 3/2 Co(II) ions has been investigated, …
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
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 …