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• W2014208564 abstract "Guanosine triphosphate and formycin triphosphate (FTP) in the presence of excess Mg2+ can bind to empty non-catalytic sites of spinach chloroplast ATPase (CF1). This results in a greatly reduced capacity for ATP hydrolysis compared to the enzyme with non-catalytic sites filled with ATP. With two GTP bound at non-catalytic sites the inhibition is about 90%; with two FTP bound about 80% inhibition is obtained. Binding and release of the nucleotides from the non-catalytic sites are relatively slow processes. Exposure of CF1 with one or two empty non-catalytic sites to 5-10 microM FTP or GTP for 15 min suffices for about 50% of the maximum inhibition. Reactivation of CF1 after exposure to higher FTP or GTP concentrations requires long exposure to 2 microM EDTA. The findings show that, contrary to previous assumptions, GTP can bind tightly to non-catalytic sites of CF1. They suggest that the presence of adenine nucleotides at non-catalytic sites might be essential for high catalytic capacity of the F1 ATPases." @default.
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• W2014208564 date "1990-09-17" @default.
• W2014208564 modified "2023-10-13" @default.
• W2014208564 title "Guanosine and formycin triphosphates bind at non-catalytic nucleotide binding sites of CF₁ATPase and inhibit ATP hydrolysis" @default.
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• W2014208564 doi "https://doi.org/10.1016/0014-5793(90)81264-o" @default.
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