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THE ACTIVE-SITES OF THE NATIVE CYTOCHROME-C-OXIDASE FROM BOVINE HEART-MITOCHONDRIA - EXAFS-SPECTROSCOPIC CHARACTERIZATION OF A NOVEL HOMOBINUCLEAR COPPER CENTER (CU-A) AND OF THE HETEROBINUCLEAR FE-A3-CU-B CENTER

被引：53
作者：
HENKEL, G
MULLER, A
WEISSGRABER, S
BUSE, G
SOULIMANE, T
STEFFENS, GCM
NOLTING, HF
机构：
[1] RHEIN WESTFAL TH AACHEN KLINIKUM,INST BIOCHEM,AACHEN,GERMANY
[2] DESY,EUROPEAN MOLEC BIOL LAB,OUTSTN HAMBURG,W-2000 HAMBURG,GERMANY
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH | 1995年 / 34卷 / 13-14期
关键词：
CYTOCHROME-C OXIDASE; METALLOENZYMES; X-RAY ABSORPTION SPECTROSCOPY;
D O I：
10.1002/anie.199514881
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fea3‐CuB center was likewise determined. (Figure Presented.) Copyright © 1995 by VCH Verlagsgesellschaft mbH, Germany
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页码：1488 / 1492
页数：5
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