Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

被引：100

作者：

Roldán, MD

Sears, HJ

Cheesman, MR

Ferguson, SJ

Thomson, AJ

Berks, BC

Richardson, DJ ^{[1
]}

机构：

[1] Univ E Anglia, Ctr Metalloprot Spect & Biol, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England

[2] Univ E Anglia, Ctr Metalloprot Spect & Biol, Sch Chem Sci, Norwich NR4 7TJ, Norfolk, England

[3] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1998年 / 273卷 / 44期

关键词：

D O I：

10.1074/jbc.273.44.28785

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：

lNapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein, Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.

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收藏

页码：28785 / 28790

页数：6

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