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X-ray absorption spectroscopic evidence for binding of the competitive inhibitor 2-mercaptoethanol to the nickel sites of Jack bean urease. A new Ni-Ni interaction in the inhibited enzyme

Journal Article · · Inorganic Chemistry; (USA)
DOI:https://doi.org/10.1021/ic00329a002· OSTI ID:6910362
;  [1];  [2]
  1. Dartmouth College, Hanover, NH (USA)
  2. Univ. of Georgia, Athens (USA)
The enzyme Jack bean urease has been identified as the first nickel-containing metalloenzyme to catalyze the hydrolysis of urea to carbon dioxide and ammonia. Competitive inhibitors such as 2-mercaptoethanol (2-ME) have been shown to dramatically affect the ground-state electronic properties of the urease Ni(II) ions. Results of preliminary structural investigations using x-ray absorption spectroscopy of the nickel salts of urease in its native and 2-ME bound forms are presented. The binding of 2-ME to Ni(II) through the thiolate sulfur is confirmed by the results of this study. 17 refs., 2 figs., 2 tabs.
DOE Contract Number:
AC03-82ER13000
OSTI ID:
6910362
Journal Information:
Inorganic Chemistry; (USA), Journal Name: Inorganic Chemistry; (USA) Vol. 29:4; ISSN 0020-1669; ISSN INOCA
Country of Publication:
United States
Language:
English