The nickel ion environment in jack bean urease.
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.
D007887:Fabaceae; D008958:Models, Molecular; D009532:Nickel / Q000032:analysis*; D010944:Plants / Q000201:enzymology*; D010946:Plants, Medicinal; D011487:Protein Conformation; D013057:Spectrum Analysis; D014510:Urease; D014965:X-Rays
D009532:Nickel; D014510:Urease