Several classes of binding sites for metals and nucleotides on yeast mitochondrial oligomycin sensitive ATPase.

Abstract:

:The binding properties of Mg2+, Mn2+ and Co2+ to yeast mitochondrial oligomycin sensitive ATPase complex are studied, as reflected by their catalytic effect (hydrolysis of ATP or pNPP, a pseudo substrate) or by a physical parameter (atomic absorption, electron paramagnetic reasonance of Mn2+, enhanced fluorescence of chelating chlorotetracyclin). At least two classes of sites with very different affinities respectively around 10(-5) M and 10(-4) M are demonstrated: high affinity sites for cations which participate in pNPP hydrolysis and can bind ADP or ATP, although they have a poor efficiency for ATP hydrolysis, and low affinity sites for cations which participate efficiently in both pNPP and ATP hydrolysis. The possibility that the tight site class has itself two sub-classes is also discussed.

journal_name

Biochimie

journal_title

Biochimie

authors

Jallon JM,Spyridakis A,Cosson J

doi

10.1016/s0300-9084(78)80701-9

keywords:

subject

Has Abstract

pub_date

1977-01-01 00:00:00

pages

869-75

issue

11-12

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(78)80701-9

journal_volume

59

pub_type

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