Abstract
The rates of hydrogen-deuterium exchange in the peptide groups of the alpha and beta subunits and the alpha-beta subunit complex of proton-translocating adenosine triphosphatase from the thermophilic bacterium PS3 were examined. The exchange was found to be much slower in the isolated beta subunit than in the isolated alpha subunit. This has been taken as indicating that the structure of the beta subunit is tighter than that of the alpha subunit. Adenosine 5'-triphosphate (ATP) caused tightening of a relatively tight portion of the alpha subunit and of a relatively loose portion of the beta subunit. When the alpha and beta subunits are brought into contact, tightening of the alpha subunit, but not the beta subunit, occurs. The effect of ATP on the structure of the beta subunit is more pronounced in the presence of the alpha subunit than in its absence. These findings support the idea proposed previously that the alpha subunit has an allosteric site and the beta subunit a catalytic site and that the conformation of the beta subunit is controlled by the alpha subunit.
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