Identification of an essential β chain lysine residue from bovine heart mitochondrial ATPase specifically modified with nitrobenzofurazan

FEBS Letters

Ferguson, Stuart J.¹  Sutton, Raul¹ 

[1] Department of Biochemistry, University of Birmingham, PO Box 363, Birmingham BIS 2TT, England

关键词: Mitochondrial ATP synthase;    Chemical modification;    Peptide purification;    Intramolecular shift F0F1-ATPase inhibition;    4-Chloro-7-nitrobenzofurazan;    Nbf-Cl;    4-chloro-7-nitrobenzofurazan;    Nbf;    nitrobenzofurazan;   

DOI  :  10.1016/0014-5793(85)80535-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A tetrapetide containing an essential lysine residue chemically modified with the nitrobenzofurazan group has been purified from bovine heart mitochondrial ATPase. The composition of the peptide indicates that this lysine is residue 401 in the sequence of a β chain. The modification was achieved by incubation at pH 9 of ATPase that had been previously labelled on a single essential tyrosine residue by reaction of the enzyme with 4-chloro-7-nitrobenzofurazan. The specific transfer of the nitrobenzofurazan group from the tyrosine residue to a particular lysine residue is consistent with the previously demonstrated intramolecular character of this transfer reaction.

【 授权许可】

Unknown