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

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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

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

Content Provider	Springer Nature Link
Author	Darrouzet, Elisabeth Valkova Valchava, Maria Ohnishi, Tomoko Daldal, Fevzi
Copyright Year	1999
Abstract	The ubiquinol: cytochrome c oxidoreductase, or the bc $_{1}$ complex, is a key component ofboth respiratory and photosynthetic electron transfer and contributes to the formation of anelectrochemical gradient necessary for ATP synthesis. Numerous bacteria harbor a bc $_{1}$ complexcomprised of three redox-active subunits, which bear two b-type hemes, one c-type heme, andone [2Fe–2S] cluster as prosthetic groups. Photosynthetic bacteria like Rhodobacter speciesprovide powerful models for studying the function and structure of this enzyme and are beingwidely used. In recent years, extensive use of spontaneous and site-directed mutants and theirrevertants, new inhibitors, discovery of natural variants of this enzyme in various species, andengineering of novel bc $_{1}$ complexes in species amenable to genetic manipulations have providedus with a wealth of information on the mechanism of function, nature of subunit interactions,and assembly of this important enzyme. The recent resolution of the structure of variousmitochondrial bc $_{1}$ complexes in different crystallographic forms has consolidated previousfindings, added atomic-scale precision to our knowledge, and raised new issues, such as thepossible movement of the Rieske Fe–S protein subunit during Q$_{o}$ site catalysis. Here, studiesperformed during the last few years using bacterial bc $_{1}$ complexes are reviewed briefly andongoing investigations and future challenges of this exciting field are mentioned.
Starting Page	275
Ending Page	288
Page Count	14
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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The Role of the Supernumerary Subunit of Rhodobactersphaeroides 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

Subunit Composition, Structure, and Distribution of Bacterial V-Type ATPases

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

The road to the crystal structure of the cytochrome bc $_{1}$ complex from the anoxigenic, photosynthetic bacterium Rhodobacter sphaeroides

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

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

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

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