Document Detail


Cytochrome b561 catalyzes transmembrane electron transfer.
MedLine Citation:
PMID:  6330096     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Purified cytochrome b561 from bovine adrenal medulla chromaffin vesicles has been reconstituted into phosphatidylcholine vesicles by a detergent-dialysis method. When the reconstituted cytochrome-containing vesicles were preloaded with ascorbic acid and cytochrome c was added to the external medium, the internal ascorbic acid was able to reduce the external cytochrome c. This reduction of cytochrome c was dependent on the presence of cytochrome b561 in the membrane and was not due to leakage of ascorbate from the vesicles. These results demonstrate that cytochrome b561 catalyzes a transmembrane electron transfer.
Authors:
M Srivastava; L T Duong; P J Fleming
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  259     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1984 Jul 
Date Detail:
Created Date:  1984-08-20     Completed Date:  1984-08-20     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8072-5     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adrenal Medulla / metabolism
Animals
Ascorbic Acid / metabolism
Chromaffin Granules / metabolism*
Chromaffin System / metabolism*
Cytochrome b Group / metabolism*
Cytochrome c Group / metabolism
Electron Transport
Intracellular Membranes / metabolism*
Kinetics
Oxidation-Reduction
Trypsin / pharmacology
Grant Support
ID/Acronym/Agency:
GM 27695/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Cytochrome b Group; 0/Cytochrome c Group; 11130-51-1/cytochrome b561; 50-81-7/Ascorbic Acid; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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