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Effect of excess cadmium ion on the metal binding site of cabbage histidinol dehydrogenase studied by 113 Cd‐NMR spectroscopy
Author(s) -
Kanaori Kenji,
Ohta Daisaku,
Nosaka Atsuko Y.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00765-5
Subject(s) - cadmium , chemistry , metal , nuclear magnetic resonance spectroscopy , spectroscopy , ion , inorganic chemistry , stereochemistry , organic chemistry , physics , quantum mechanics
The enzymatic reaction of histidinol dehydrogenase (HDH) was stimulated by about maximally 75% on the addition of Cd 2+ ion to the reaction mixture. 113 Cd‐substituted HDH in the presence of excess Cd 2+ has been studied by 113 Cd‐NMR. 113 Cd 2+ less than 1 equiv. per subunit preferentially binds to the catalytic metal binding site of the apoenzyme. Further addition of the metal ions causes the structural change of the enzyme including the catalytic metal binding site. HDH takes at least three discernible states, which may correspond to the more or less active forms of the enzyme induced by metal ions.