IDENTIFICATION OF THE AXIAL HEME LIGANDS OF CYTOCHROME B(556) IN SUCCINATE - UBIQUINONE OXIDOREDUCTASE FROM ESCHERICHIA-COLI

被引：35

作者：

PETERSON, J ^{[1
]}

VIBAT, C ^{[1
]}

GENNIS, RB ^{[1
]}

机构：

[1] UNIV ILLINOIS, SCH CHEM SCI, URBANA, IL 61801 USA

来源：

FEBS LETTERS | 1994年 / 355卷 / 02期

关键词：

HEME PROTEIN; AXIAL LIGAND; EPR; MCD; SUCCINATE DEHYDROGENASE;

D O I：

10.1016/0014-5793(94)01189-3

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 paramagnetic resonance (EPR) and near-infrared magnetic circular dichroism (MCD) have been used to identify the ligands to the cytochrome b(556) component of succinate: ubiquinone oxidoreductase (succinate dehydrogenase) from Escherichia coli. The 'highly axial low spin' (HALS) EPR spectrum suggests bis(histidine) ligation of the heme with the histidines in a staggered configuration. The near-infrared MCD spectrum exhibits a low energy maximum at 1600 nm which is also clearly indicative of bis(histidine) ligation of the heme iron. The data unambiguously demonstrate that the heme b(556) is ligated to E. coli succinate dehydrogenase via two histidines.

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页码：155 / 156

页数：2

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