Document Detail


Protein conformational changes involved in the cytochrome bc1 complex catalytic cycle.
MedLine Citation:
PMID:  23876289     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Early structures of the cytochrome bc1 complex revealed heterogeneity in the position of the soluble portion of the Rieske iron sulfur protein subunit, implicating a movement of this domain during function. Subsequent biochemical and biophysical works have firmly established that the motion of this subunit acts in the capacity of a conformationally assisted electron transfer step during the already complicated catalytic mechanism described within the modified version of Peter Mitchells Q cycle. How the movement of this subunit is initiated or how the frequency of its motion is controlled as a function of other steps during the catalysis remain topics of debate within the active research communities. This review addresses the historical aspects of the discovery and description of this movement, while attempting to provide a context for the involvement of conformational motion in the catalysis and efficiency of the enzyme. This article is part of a Special Issue entitled: Respiratory complex III and related bc complexes.
Authors:
Jason W Cooley
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-7-20
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  -     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2013 Jul 
Date Detail:
Created Date:  2013-7-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2013.
Affiliation:
Department of Chemistry, University of Missouri, Columbia, MO 65211-7600, USA. Electronic address: cooleyjw@missouri.edu.
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