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The nickel ion environment in jack bean urease

Authors :
Alagna, L
Hasnain, S S
Piggott, B
Williams, D J
Source :
Biochemical Journal; June 1984, Vol. 220 Issue: 2 p591-595, 5p
Publication Year :
1984

Abstract

Preliminary results of an extended X-ray absorption fine structure (e.x.a.f.s.) and X-ray absorption near edge structure study of jack bean urease have recently been reported [Hasnain & Piggott (1983) Biochem. Biophys. Res. Commun. 112, 279]. These results indicate that the environment of the nickel ion in the enzyme is similar to that in the model compounds Ni(L)2(L')1(ClO4)1 (where L is 1-n-propyl-2-alpha-hydroxybenzylbenzimidazole and L' is the deprotonated form) and Ni(HMB)3(Br)2 (where HMB is 2-hydroxymethylbenzimidazole), the closest similarity being with Ni(L)2-(L')1(ClO4)1. A detailed e.x.a.f.s. analysis has now been carried out and the crystal structures of the two model compounds solved. These results are reported here.

Details

Language :
English
ISSN :
02646021 and 14708728
Volume :
220
Issue :
2
Database :
Supplemental Index
Journal :
Biochemical Journal
Publication Type :
Periodical
Accession number :
ejs51297120
Full Text :
https://doi.org/10.1042/bj2200591