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
Biochimiejournal_title
Biochimieauthors
Jallon JM,Spyridakis A,Cosson Jdoi
10.1016/s0300-9084(78)80701-9keywords:
subject
Has Abstractpub_date
1977-01-01 00:00:00pages
869-75issue
11-12eissn
0300-9084issn
1638-6183pii
S0300-9084(78)80701-9journal_volume
59pub_type
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