Observations concerning the quinol oxidation site of the cytochrome bc{sub 1} complex
Journal Article
·
· Federation of European Biochemical Societies
- LBNL Library
A direct hydrogen bond between ubiquinone/quinol bound at the QO 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, 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 bc1 complex.
- Research Organization:
- Ernest Orlando Lawrence Berkeley National Laboratory, Berkeley, CA (US)
- Sponsoring Organization:
- US Department of Energy; National Institute of Health Grant DK44842 (US)
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 832755
- Report Number(s):
- LBNL--53853
- Journal Information:
- Federation of European Biochemical Societies, Journal Name: Federation of European Biochemical Societies Journal Issue: 1 Vol. 555
- Country of Publication:
- United States
- Language:
- English
Similar Records
The Architecture of the Qo Site of Cytochrome bc1 Complex Probed by Superoxide Production
The Inhibitor DBMIB Provides Insight into the Functional Architecture of the Qo Site in the Cytochrome b(6)f Complex
The Raised Midpoint Potential of the[2Fe2S] Cluster of Cytochrome bc1 is Mediated by Both the Q(o) Site Occupants and the Head Domain Position of the Fe-S Protein Subunit
Journal Article
·
Tue Jun 03 00:00:00 EDT 2003
· Biochemistry
·
OSTI ID:15005590
The Inhibitor DBMIB Provides Insight into the Functional Architecture of the Qo Site in the Cytochrome b(6)f Complex
Journal Article
·
Tue Jun 22 00:00:00 EDT 2004
· Biochemistry
·
OSTI ID:15008816
The Raised Midpoint Potential of the[2Fe2S] Cluster of Cytochrome bc1 is Mediated by Both the Q(o) Site Occupants and the Head Domain Position of the Fe-S Protein Subunit
Journal Article
·
Mon Mar 01 23:00:00 EST 2004
· Biochemistry (Eaton)
·
OSTI ID:15007033