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- W36173664 abstract "The optical properties of the cobalt substituted alcohol dehydrogenases have been monitored in an effort to definitely establish the correlation between the fast and slow exchanging metal with the catalytic and structural sites. The visible spectra of the substituted enzyme and the binary and ternary complexes of the enzyme with coenzymes and substrate inhibitors were measured as a function of the cobalt ions incorporated in the enzyme. Optical spectra were recorded at 77° in addition to 298° to increase the spectral resolutions, and were compared to spectra of model compounds involving cobalt (II) in order to make specific spectral assignments and to predict the geometry and composition of the ligand field of the metal ions. This chapter discusses kinetics of the exchange of cobalt ions for zinc ions in alcohol dehydrogenase and effect of differing cobalt levels on optical spectra at 77°." @default.
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- W36173664 date "1977-01-01" @default.
- W36173664 modified "2023-09-23" @default.
- W36173664 title "ROOM AND LOW TEMPERATURE SPECTRAL IDENTIFICATION OF THE COBALT BINDINGS SITES IN LIVER ALCOHOL DEHYDROGENASE" @default.
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- W36173664 doi "https://doi.org/10.1016/b978-0-12-691402-3.50014-7" @default.
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