Q-BAND ENDOR SPECTRA OF THE RIESKE PROTEIN FROM RHODOBACTOR-CAPSULATUS UBIQUINOL CYTOCHROME-C OXIDOREDUCTASE SHOW 2 HISTIDINES COORDINATED TO THE [2FE-2S] CLUSTER

被引：87

作者：

GURBIEL, RJ

OHNISHI, T

ROBERTSON, DE

DALDAL, F

HOFFMAN, BM

机构：

[1] NORTHWESTERN UNIV,DEPT CHEM,EVANSTON,IL 60208

[2] JAGIELLONIAN UNIV,INST MOLEC BIOL,PL-31007 KRAKOW,POLAND

[3] UNIV PENN,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104

[4] UNIV PENN,DEPT BIOL,PHILADELPHIA,PA 19104

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 49期

关键词：

D O I：

10.1021/bi00113a013

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：

Electron nuclear double resonance (ENDOR) experiments were performed on N-14 (natural abundance) and N-15-enriched iron-sulfur Rieske protein in the ubiquinol-cytochrome c2 oxidoreductase from Rhodobacter capsulatus. The experiments proved that two distinct nitrogenous ligands, histidines, are undoubtedly ligated to the Rieske [2Fe-2S] center. The calculations of hyperfine tensors give values similar but not identical to those of the Rieske-type cluster in phthalate dioxygenase of Pseudomonas cepacia and suggest a slightly different geometry of the iron-sulfur cluster in the two proteins.

引用

页码：11579 / 11584

页数：6

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