Observations concerning the quinol oxidation site of the cytochrome bc 1 complex

FEBS Letters

Huang, Li-shar¹  Berry, Edward A.¹ 

[1]MS 64R121, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

关键词: Ubiquinone;    Cytochrome c;    Oxidoreductase;    Membrane protein complex;    Respiratory enzyme;    Protein crystal;    X-ray;    Structure;    Mechanism;    Tautomerism;    Resonance;    cyt.;    cytochrome;    EPR;    electron paramagnetic resonance;    QO;    quinol oxidation site proposed by protonmotive Q-cycle hypothesis;   

DOI  :  10.1016/S0014-5793(03)01099-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A direct hydrogen bond between ubiquinone/quinol bound at the Q_O site and a cluster-ligand histidine of the iron–sulfur protein (ISP) is described as a major determining factor explaining much experimental data on position of the ISP ectodomain, electron paramagnetic resonance (EPR) lineshape and midpoint potential of the iron–sulfur cluster, and the mechanism of the bifurcated electron transfer from ubiquinol to the high and low potential chains of the bc ₁ complex.

【 授权许可】

Unknown