Characterisation of phosphate binding to mitochondrial and bacterial membrane‐bound ATP synthase by studies of inhibition with 4‐chloro‐7‐nitrobenzofurazan

FEBS Letters

Greenfield, Anthony J.¹  Perez, Juan A.¹  Ferguson, Stuart J.¹  Sutton, Raul¹ 

[1] Department of Biochemistry, University of Birmingham, PO Box 363, Birmingham B15 2TT England

关键词: ATP synthase;    Phosphate binding;    Chemical modification;    Tyrosine residue;   

DOI  :  10.1016/0014-5793(86)81195-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of phosphate on the inhibition by 4-chloro-7-nitrobenzofurazan of the ATPase activity of the proton-translocating ATP synthase in heart submitochondrial particles was investigated. Binding of phosphate protected strongly against the inhibition. A dissociation constant of 0.2 mM was determined for the enzyme · P_i complex and shown to be independent of pH in the range 7.0–8.0. The protective effect of phosphate was mimicked by arsenate but not by sulphate or malonate. Similar results were obtained for the enzyme from Paracoccus denitrificans. 2,4-Dinitrophenol enhanced phosphate binding to the mitochondrial enzyme since the protective effect of phosphate was increased. The data are compatible with protection arising from binding of phosphate to a catalytic site.

【 授权许可】

Unknown