Document Detail


Differential labeling of the subunits of respiratory complex III with [3H]succinic anhydride, [14C]succinic anhydride, and p-diazobenzene-[35S]sulfonate.
MedLine Citation:
PMID:  3007448     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Exposure of antimycin-treated Complex III (ubiquinol-cytochrome c reductase) purified from bovine heart mitochondria to [3H]succinic anhydride plus [35S]p-diazobenzenesulfonate (DABS) resulted in somewhat uniform relative labeling of the eight measured subunits of the complex by [3H]succinic anhydride. In contrast, relative labeling by [35S]DABS was similar to [3H]succinic anhydride for the subunits of high molecular mass, i.e., core proteins, cytochromes, and the iron-sulfur protein, but greatly reduced for the polypeptides of molecular mass below 15 kDa. With Complex II depleted in the iron-sulfur protein the relative labeling of core protein I by exposure of the complex to [3H]succinic anhydride was significantly enhanced, whereas labeling of the polypeptides represented by SDS-PAGE bands 7 and 8 was significantly inhibited. Dual labeling of the subunits of Complex III by 14C- and 3H-labeled succinic anhydride before and after dissociation of the complex by sodium dodecyl sulfate, respectively, was measured with the complex in its oxidized, reduced, and antimycin-inhibited states. Subunits observed to be most accessible or reactive to succinic anhydride were core protein II, the iron-sulfur protein, and polypeptides of SDS-PAGE bands 7,8, and 9. Two additional polypeptides of molecular masses 23 and 12kDa, not normally resolved by gel-electrophoresis, were detected. Reduction of the complex resulted in a significant change of 14C/3H labeling ratio of core protein only, whereas treatment of the complex with antimycin resulted in decreases in 14C/3H labeling ratios of core proteins I and II, cytochrome c1, and a polypeptide of molecular mass 13kDa identified as an antimycin-binding protein.
Authors:
S H Ho; J S Rieske
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of bioenergetics and biomembranes     Volume:  17     ISSN:  0145-479X     ISO Abbreviation:  J. Bioenerg. Biomembr.     Publication Date:  1985 Dec 
Date Detail:
Created Date:  1986-05-05     Completed Date:  1986-05-05     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7701859     Medline TA:  J Bioenerg Biomembr     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  333-48     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Antimycin A / pharmacology
Benzenesulfonates / metabolism*
Carbon Radioisotopes
Cattle
Diazonium Compounds / metabolism*
Electron Transport Complex III
Electrophoresis, Polyacrylamide Gel
Iron-Sulfur Proteins / metabolism
Mitochondria, Heart / metabolism*
Multienzyme Complexes / metabolism*
Oxidation-Reduction
Protein Conformation
Quinone Reductases / metabolism*
Succinates / metabolism*
Succinic Anhydrides / metabolism*
Sulfanilic Acids / metabolism*
Tritium
Grant Support
ID/Acronym/Agency:
HL-265298/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Benzenesulfonates; 0/Carbon Radioisotopes; 0/Diazonium Compounds; 0/Iron-Sulfur Proteins; 0/Multienzyme Complexes; 0/Rieske iron-sulfur protein; 0/Succinates; 0/Succinic Anhydrides; 0/Sulfanilic Acids; 10028-17-8/Tritium; 2154-66-7/diazobenzenesulfonic acid; 642-15-9/Antimycin A; EC 1.10.2.2/Electron Transport Complex III; EC 1.6.99.-/Quinone Reductases

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


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