pH dependent conformational changes modulate functional activity of the mitochondrial ATPase inhibitor protein.

Abstract:

:A 12kDa, heat stable protein (IF1) inhibiting hydrolytic activity of submitochondrial particles was purified to electrophoretic homogeneity from buffalo heart mitochondria. Specific activity of the purified fraction was > 5000 units/mg. Maximal inhibition was observed at pH 6.0 and was Mg++ and ATP dependent. Circular dichroism studies showed that the inhibitor peptide undergoes a dramatic, reversible conformational change in response to pH which correlates well with its ability to inhibit ATP hydrolysis catalyzed by inhibitor depleted submitochondrial particles. It is shown for the first time that IF1 with a predominantly beta-sheet component is more efficient at suppressing ATPase activity.

authors

Sah JF,Kumar C,Mohanty P

doi

10.1006/bbrc.1993.1997

subject

Has Abstract

pub_date

1993-08-16 00:00:00

pages

1521-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71997-2

journal_volume

194

pub_type

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