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 · Wed Feb 21 00:00:00 EST 1990 · Inorganic Chemistry; (USA)

DOI:https://doi.org/10.1021/ic00329a002· OSTI ID:6910362

Clark, P A; Wilcox, D E ^[1]; Scott, R A ^[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), Vol. 29:4; ISSN 0020-1669
• Country of Publication: United States
• Language: English

Related Subjects

10 SYNTHETIC FUELS
AMMONIA
CHEMICAL PREPARATION
NICKEL COMPLEXES
STRUCTURAL CHEMICAL ANALYSIS
ORGANOMETALLIC COMPOUNDS
UREA
HYDROLYSIS
UREASE
ABSORPTION SPECTROSCOPY
CATALYSIS
EXPERIMENTAL DATA
PLANTS
X RADIATION
AMIDES
AMIDINASES
CARBONIC ACID DERIVATIVES
CHEMICAL REACTIONS
COMPLEXES
DATA
DECOMPOSITION
ELECTROMAGNETIC RADIATION
ENZYMES
HYDRIDES
HYDROGEN COMPOUNDS
HYDROLASES
INFORMATION
IONIZING RADIATIONS
LYSIS
NITROGEN COMPOUNDS
NITROGEN HYDRIDES
NON-PEPTIDE C-N HYDROLASES
NUMERICAL DATA
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
RADIATIONS
SOLVOLYSIS
SPECTROSCOPY
SYNTHESIS
TRANSITION ELEMENT COMPLEXES
100200* - Synthetic Fuels- Production- (1990-)