Binding of TNP-ATP and TNP-ADP to the non-catalytic sites ofEscherichia coliF1-ATPase
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The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase.
The ribose-modified nucleotides 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and TNP-ADP were used to probe the catalytic sites on soluble beef heart mitochondrial adenosine triphosphatase (F1). Both compounds were potent competitive inhibitors of ATP hydrolysis catalyzed by F1, Ki = 5.5 and 10 nM, respectively, and by submitochondrial particles, Ki (TNP-ATP) = 21 nM. Both...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1997
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(97)00773-4