THE SUBSTRATE-BINDING SITE IN CU NITRITE REDUCTASE AND ITS SIMILARITY TO ZN CARBONIC-ANHYDRASE

被引：70

作者：

STRANGE, RW

DODD, FE

ABRAHAM, ZHL

GROSSMANN, JG

BRUSER, T

EADY, RR

SMITH, BE

HASNAIN, SS

机构：

[1] SERC, DARESBURY LAB, MOLEC BIOPHYS GRP, WARRINGTON WA4 4AD, CHESHIRE, ENGLAND

[2] DE MONTFORT UNIV, LEICESTER LE1 9BH, LEICS, ENGLAND

[3] UNIV SUSSEX, NITROGEN FIXAT LAB, BRIGHTON BN1 9RQ, E SUSSEX, ENGLAND

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 04期

关键词：

D O I：

10.1038/nsb0495-287

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Here we investigate the structure of the two types of copper site in nitrite reductase from Alcaligenes xylosoxidans, the molecular organisation of the enzyme when the type-2 copper is absent, and its mode of substrate binding. X-ray absorption studies provide evidence for a fourth ligand at the type-2 Cu, that substrate binds to this site and indicates that this binding does not change the type-1 Cu centre. The substrate replaces a putative water ligand and is accommodated by a lengthening of the Cu-histidine bond by approximately 0.08 Angstrom. Modelling suggests a similarity between this unusual type-2 Cu site and the Zn site in carbonic anhydrase and that nitrite is anchored by hydrogen bonds to an unligated histidine present in the type-2 Cu cavity.

引用

页码：287 / 292

页数：6

共 42 条

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