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2,2-Dipyridyl binding to metal substituted horse liver alcohol dehydrogenase

Authors
Journal
Journal of Inorganic Biochemistry
0162-0134
Publisher
Elsevier
Publication Date
Volume
22
Issue
1
Identifiers
DOI: 10.1016/0162-0134(84)85062-x
Disciplines
  • Biology

Abstract

Abstract The binding of 2,2-dipyridyl to metal substituted horse liver alcohol dehydrogenase was measured by spectrophotometric titrations. Large changes in the visible absorption spectra were seen for the Co 2+, Cu 2+ and Ni 2+ hybrids upon coordination of 2,2-dipyridyl, due to a change in coordination number. The formation constants for binding to the Co 2+ and Cd 2+ hybrids are of the order 10 6 M −1, which means that these hybrids have a 500-fold higher affinity for 2,2-dipyridyl than the native Zn 2+ enzyme. 2,2-dipyridyl has a 100-fold higher affinity for enzyme bound Cd 2+ than for aqueous Cd 2+ ions, while for Cu 2+ and Zn 2+ the opposite is the case. None of the substituted metal ions were removed from the active site during titration with the chelator 2,2-dipyridyl.

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