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Catalytic properties of beef heart mitochondrial ATPase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Evidence for catalytic site cooperativity during ATP synthesis


Catalytic properties of beef heart mitochondrial ATPase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Evidence for catalytic site cooperativity during ATP synthesis



Journal of Biological Chemistry 257(7): 3441-3446



ISSN/ISBN: 0021-9258

PMID: 6460767

The incorporation of water oxygens into the .gamma.-phosphoryl group of ATP during ATP synthesis (intermediate ATP .dblarw. HOH exchange) was studied in a preparation of mitochondrial inner membranes reconstituted with F1-ATPase modified by NBD-Cl (7-chloro-4-nitrobenzo-2-oxa-1,3-diazole). These particles allow ATP synthesis although ATP hydrolysis is largely blocked. The incorporation of water oxygens into each ATP molecule synthesized increased significantly as the medium ADP concentration was lowered, as has been observed with native mitochondrial and chloroplast membranes. However, at each ADP concentration tested, the extent of exchange was less than that catalyzed by control preparations that were not modified by NBD-Cl. Further, the concentration of ADP required for a half-maximal rate of ATP synthesis (S0.5) is .apprx. 10-fold greater than that observed with native submitochondrial particles. The effects of NBD-Cl probably are not limited to ATP hydrolysis. More importantly, although the NBD group appears to alter the catalytic properties, alternating or sequential catalytic sites are still participating in a coordinated manner consistent with the binding-change mechanism for ATP synthesis. The effects of NBD-Cl treatment cannot be taken as evidence for participation of separate catalytic sites or loci in ATP synthesis and hydrolysis. A residual ATPase activity observed in the presence of NBD-Cl results largely from a slow, spontaneous reactivation process that can be observed after removal of medium NBD-Cl.

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Accession: 004887180

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