[Functions and localization of nucleotide-binding sites of CF1-ATPase using dialdehyde derivatives of ADP and ATP].
The covalent binding of dialdehyde derivatives of ATP and ADP (o-ATP and o-ADP) results in inactivation of chloroplast CF1-ATPase, the degree of inactivation being increased at a rise in temperature and pH. o-ADP causes predominant inhibition of the Mg2+-dependent, while o-ATP--of both Mg2+- and Ca2+-dependent activities of CF1-ATPase. The substrates and reaction products prevent the enzyme inactivation, whereas the stimulators of the Mg2+-dependent ATPase activity enhance it. The effect of these stimulators is correlated with predominant incorporation of [3H] o-nucleotide into the beta-subunit of CF1. In the absence of the stimulators o-ADP is predominantly bound to the alpha-subunit of CF1. The binding of o-ADP and o-ATP to the beta-subunit is increased in the presence of Mg2+. A comparative analysis of the labelled nucleotides incorporation into individual subunits and the changes in the catalytic and regulatory properties of the enzyme demonstrated that the catalytic and stimulator-sensitive "regulatory" sites of the enzyme are located on the beta-subunits.
D000244:Adenosine Diphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D002736:Chloroplasts / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D010944:Plants / Q000201:enzymology; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D046911:Macromolecular Substances; C017199:2',3'-dialdehyde ATP; D000244:Adenosine Diphosphate; C018808:adenosine 5'-diphosphate 2',3'-dialdehyde; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D008274:Magnesium; D002118:Calcium
Issledovanie funktsiĭ i lokalizatsii nukleotidsviazyvaiushchikh tsentrov CF1-ATPazy s pomoshch'iu dial'degidnykh proizvodnykh ADP i ATP.