| Cytochrome b561 catalyzes transmembrane electron transfer. | |
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MedLine Citation:
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PMID: 6330096 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M Srivastava; L T Duong; P J Fleming |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 259 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1984 Jul |
Date Detail:
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Created Date: 1984-08-20 Completed Date: 1984-08-20 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 8072-5 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adrenal Medulla
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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:
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GM 27695/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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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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