NDLI: Primary Steps in the Energy Conversion Reaction of theCytochrome bc $

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Comparison of the Cytochrome bc $_{1}$ Complex with theAnticipated Structure of the Cytochrome b $_{6}$ f Complex:De Plus Ça Change de Plus C'est la Même Chose

The Role of Various Domains of the Iron–Sulfur Protein in the Assembly and Activity of the Cytochromme bc $_{1}$ Complex of Yeast Mitochondria

Primary Steps in the Energy Conversion Reaction of theCytochrome bc $_{1}$ Complex QO Site

Role of the Rieske Iron–Sulfur Protein Midpoint Potential in the Protonmotive Q-Cycle Mechanism of the Cytochrome bc $_{1}$ Complex

Control of Ubiquinol Oxidation at Center P (QO) of the Cytochrome bc $_{1}$ Complex

The Role of the Supernumerary Subunit of Rhodobactersphaeroides Cytochrome bc $_{1}$ Complex

Integration of the Mitochondrial-Processing Peptidase into the Cytochrome bc $_{1}$ Complex in Plants

Structure and Function of the Bacterial bc $_{1}$ Complex: Domain Movement, Subunit Interactions, and Emerging Rationale Engineering Attempts

Journal of Bioenergetics and Biomembranes : Volume 31, Issue 2, April 1999

Journal of Bioenergetics and Biomembranes : Volume 31, Issue 1, February 1999

Journal of Bioenergetics and Biomembranes : Volume 30

Journal of Bioenergetics and Biomembranes : Volume 29

Primary Steps in the Energy Conversion Reaction of theCytochrome bc $_{1}$ Complex QO Site

Content Provider	Springer Nature Link
Author	Sharp, R. Eryl Moser, Christopher C. Gibney, Brian R. Dutton, P. Leslie
Copyright Year	1999
Abstract	The primary energy conversion (Q$_{O}$) site of the cytochrome bc $_{1}$ complex is flanked by bothhigh- and low-potential redox cofactors, the [2Fe–2S] cluster and cytochrome b $_{L}$, respectively.From the sensitivity of the reduced [2Fe–2S] cluster electron paramagnetic resonance (EPR)spectral g $_{x}$-band and line shape to the degree and type of Q$_{O}$ site occupants, we have proposeda double-occupancy model for the Q$_{O}$ site by ubiquinone in Rhodobacter capsulatus membranevesicles containing the cytochrome bc $_{1}$ complex. Biophysical and biochemical experimentshave confirmed the double occupancy model and from a combination of these results and theavailable cytochrome bc $_{1}$ crystal structures we suggest that the two ubiquinone molecules inthe Q$_{O}$ site serve distinct catalytic roles. We propose that the strongly bound ubiquinone,termed Q$_{OS}$, is close to the [2Fe–2S] cluster, where it remains tightly associated with the Q$_{O}$site during turnover, serving as a catalytic cofactor; and the weaker bound ubiquinone, Q$_{OW}$,is distal to the [2Fe–2S] cluster and can exchange with the membrane Q$_{pool}$ on a time scalemuch faster than the turnover, acting as the substrate. The crystallographic data demonstratesthat the FeS subunit can adopt different positions. Our own observations show that theequilibrium position of the reduced FeS subunit is proximal to the Q$_{O}$ site. On the basis of this, wealso report preliminary results modeling the electron transfer reactions that can occur in thecytochrome bc $_{1}$ complex and show that because of the strong distance dependence of electrontransfer, significant movement of the FeS subunit must occur in order for the complex to beable to turn over at the experimental observed rates.
Starting Page	225
Ending Page	234
Page Count	10
File Format	PDF
ISSN	0145479X
Journal	Journal of Bioenergetics and Biomembranes
Volume Number	31
Issue Number	3
e-ISSN	15736881
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	1999-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Organic Chemistry Biochemistry Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology

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Control of Ubiquinol Oxidation at Center P (QO) of the Cytochrome bc $_{1}$ Complex

Structure of the Avian Mitochondrial Cytochrome bc $_{1}$ Complex

Structural Basis of Multifunctional Bovine Mitochondrial Cytochrome bc $_{1}$ Complex

Study of the Cytochrome bc $_{1}$ Complex Entering a New Phase

The Role of the Supernumerary Subunit of Rhodobactersphaeroides Cytochrome bc $_{1}$ Complex

Conformational Change of the Rieske [2Fe–2S] Protein inCytochrome bc $_{1}$ Complex

Integration of the Mitochondrial-Processing Peptidase into the Cytochrome bc $_{1}$ Complex in Plants

Steady-State Proton Translocation in Bovine Heart Mitochondrial bc $_{1}$ Complex Reconstituted into Liposomes

Breaking the Q-cycle: finding new ways to study Qo through thermodynamic manipulations

Primary Steps in the Energy Conversion Reaction of theCytochrome bc $_{1}$ Complex QO Site

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Primary Steps in the Energy Conversion Reaction of theCytochrome bc $_{1}$ Complex QO Site