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- W2480334380 abstract "In metalloenzymes, metals which affect function directly by participation in catalysis appear to have ligand sites which differ markedly from those of metals which influence function indirectly through modulation of protein structure. Thus, in both E. coli alkaline phosphatase and equine liver alcohol dehydrogenase, metals positioned at the active site interact selectively with chelating agents, undergo isotope exchange, and display distinctive physical chemical characteristics. Such active site metals may have an irregular geometry which facilitates their catalytic role. In contrast, nonactive site metals exhibit physical properties more like those of simple, bidentate model complexes; they frequently appear to stabilize structure or influence subunit interactions as shown by their effects on sedimentation or hydrogen exchange rates of proteins. Such structural metals may function importantly in control mechanisms for biochemical reactions." @default.
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- W2480334380 date "1971-06-01" @default.
- W2480334380 modified "2023-10-06" @default.
- W2480334380 title "Structure and Function of Metalloenzymes" @default.
- W2480334380 doi "https://doi.org/10.1021/ba-1971-0100.ch010" @default.
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