[ESR study of interaction between adenylate kinase, substrates and Mn2+ ions]. / Issledovanie vzaimodeistviia adenilatkinazy a substratami i ionami margantsa metodom élektronnogo paramagnitnogo rezonansa.

Plant adenylate kinase was first investigated by ESR technique at room temperature. In contrast to previous studies the measurement conditions corresponded to maximal enzyme activity. It was shown that adenylate kinase addition provoked Mn2+--adenine nucleotide binary complex distribution and rearrangement of components with the formation of ternary Mn2+--adenine nucleotide--adenylate kinase complex. The same results were obtained in the studies on myokinase from rabbit muscle.

[Analysis of ESR spectra in Mn2+-plant adenylate kinase complex]. / Analiz spektrov élektronnogo paramagnitnogo rezonansa kompleksov ionov margantsa s adenilatkinazoi rastitel'nogo proiskhozhdeniia.

Interaction of plant adenylate kinase with Mn2+-adenine nucleotide binary complex was studied by ESR technique at room temperature. The ligand environment of Mn2+ in the ternary Mn2+-adenine nucleotide-enzyme complex was shown to change, as a result of enzyme binding as compared with that of binary complex. These changes seem to be due to substitution of protein molecules for water and adenine nucleotide ones, coordinated to Mn2+ ion on ternary complex formation. The same results were obtained in ESR studies on rabbit muscle myokinase. This fact may be considered as an evidence, that plant adenylate kinase is identical to animal one in its interaction with adenine nucleotides and manganese ions.