| Reaction of cytochrome c in the electron-transport chain of Paracoccus denitrificans. | |
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MedLine Citation:
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PMID: 6315059 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The reaction of the cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) of Paracoccus denitrificans cytoplasmic membranes with the endogenous cytochrome c of the membranes was studied, as well as its interaction with added exogenous cytochrome c from P. denitrificans or bovine heart. The polarographic method was employed, using N,N,N',N'-tetramethyl-p-phenylenediamine plus ascorbate to reduce the cytochrome c. We found that overall electron transport can proceed maximally while the cytochrome c remains membrane bound; NADH or succinoxidase activities were not inhibited by the addition of substances which bind the P. denitrificans cytochrome c strongly. In contrast to our observations with the spectrophotometric method (Smith, L., Davies, H.C. and Nava, M.E. (1976) Biochemistry 15, 5827-5831), in the polarographic assays the membrane-bound oxidase reacts with about equal rapidity with exogenous bovine and P. denitrificans cytochromes c. The reaction of the oxidase with the endogenous cytochrome c proceeds at high rates and preferentially to that with exogenous cytochrome c; the reaction with the latter, but not the former is inhibited by positively charged poly(L-lysine). The cytochrome c and the oxidase appear to be very closely associated on the membrane. |
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Authors:
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H C Davies; L Smith; M E Nava |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 725 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1983 Nov |
Date Detail:
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Created Date: 1984-01-26 Completed Date: 1984-01-26 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 238-45 Citation Subset: IM |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cattle Cytochrome c Group / metabolism* Deoxycholic Acid / pharmacology Electron Transport Electron Transport Complex IV / metabolism Multienzyme Complexes / metabolism Myocardium / enzymology NADH, NADPH Oxidoreductases / metabolism Oxygen / metabolism Paracoccus denitrificans / enzymology* Tetramethylphenylenediamine / pharmacology |
| Grant Support | |
ID/Acronym/Agency:
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GM06270/GM/NIGMS NIH HHS; HL28272/HL/NHLBI NIH HHS; RR05392/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cytochrome c Group; 0/Multienzyme Complexes; 27215-51-6/Tetramethylphenylenediamine; 7782-44-7/Oxygen; 83-44-3/Deoxycholic Acid; EC 1.6.-/NADH oxidase; EC 1.6.-/NADH, NADPH Oxidoreductases; EC 1.9.3.1/Electron Transport Complex IV |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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