PMID: 3753467Jun 1, 1986Paper

Structural study of the copper and zinc sites in metallothioneins by using extended X-ray-absorption fine structure

The Biochemical Journal
I L AbrahamsM Vasák

Abstract

Zn-metallothionein 1 from rabbit liver was investigated by means of Zn K-edge extended X-ray-absorption fine structure (e.x.a.f.s.). Also, the Cu and Zn K-edge e.x.a.f.s. were measured for two samples of mixed Cu Zn-metallothionein 2, with Cu/Zn ratios of 5:2 and 6:3, from pig liver. Detailed simulation of the Cu sites shows a primary co-ordination with three sulphur atoms, presumably from cysteine residues at 0.225 nm +/- 0.001 nm (2.25 +/- 0.01 A). The data for the Zn sites are best reproduced by four Zn-S separations at 0.233 +/- 0.001 nm (2.33 +/- 0.01 A). The Zn K-edge e.x.a.f.s. recorded for rabbit metallothionein 1 at 77 K shows, in addition to the primary co-ordination shell, evidence for two Zn-Zn separations at approx. 0.50 nm (5.0 A). This latter result provides the first information concerning the internal arrangement of zinc atoms in Zn7-metallothionein.

Citations

Nov 15, 1988·Biochemistry·J H Kägi, A Schäffer
Sep 5, 1989·Biochemistry·M C Feiters, J Jeffery
Mar 1, 1996·European Journal of Biochemistry·A CorazzaP J Sadler
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Mar 30, 2004·Environmental Science & Technology·Suzanne BeaucheminJames C McGeer

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