Formation of an intramolecular disulfide bond in the mitochondrial adenine nucleotide translocase.
Adenine nucleotide translocase in electron transport particles or in H+-ATPase preparation from bovine heart mitochondria is capable of forming both inter- and intramolecular disulfide bridges upon reaction with copper-o-phenanthroline. We have examined the localisation of the intramolecular disulfide bridge in the protein chain by peptide fragmentation methods. The most likely position of the disulfide bridge is between cysteine 159 and 256, but the possibility of the presence of a second disulfide bridge formed between 129 and 256 cannot be ruled out. Our experimental results support the theoretical model proposed [(1982) FEBS Lett. 144, 250-254] for the topography of the translocase and provide a more accurate description of the arrangement of some of the hydrophilic segments in the molecule.
Torok
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Joshi
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D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003488:Cyanogen Bromide; D003545:Cysteine; D004220:Disulfides; D008929:Mitochondria, Heart / Q000201:enzymology*; D000226:Mitochondrial ADP, ATP Translocases; D009713:Nucleotidyltransferases; D010446:Peptide Fragments / Q000302:isolation & purification; D010618:Phenanthrolines / Q000494:pharmacology; D006180:Proton-Translocating ATPases
D004220:Disulfides; D010446:Peptide Fragments; D010618:Phenanthrolines; D000226:Mitochondrial ADP, ATP Translocases; D009713:Nucleotidyltransferases; D006180:Proton-Translocating ATPases; D003545:Cysteine; D003488:Cyanogen Bromide; C025205:1,10-phenanthroline