Premium
The difference between ADP‐beryllium fluoride and ADP‐aluminium fluoride complexes of the spin‐labeled myosin subfragment 1
Author(s) -
М. А. Пономарев,
Vladimir P. Timofeev,
Dmitrii I. Levitsky
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00898-j
Subject(s) - chemistry , adenosine diphosphate , electron paramagnetic resonance , fluoride , myosin , myosin atpase , atpase , phosphate , site directed spin labeling , spin label , nucleotide , crystallography , enzyme , inorganic chemistry , biochemistry , membrane , nuclear magnetic resonance , platelet aggregation , platelet , physics , gene , immunology , biology
Electron paramagnetic resonance (EPR) spectroscopy was used for investigation of the structure of spin‐labeled myosin subfragment 1 (S1) containing ADP and phosphate analogues, such as orthovanadate, aluminium fluoride (AlF 4 ), and beryllium fluoride (BeF x ). It has been shown that the local conformational changes in the region of Cys‐707, induced by formation of the S1‐ADP‐BeF x complex, differ from those of S1 containing ADP‐AlF 4 or other phosphate analogues but are similar to the changes which occur in the presence of ADP or ATPγS. It is suggested that S1‐ADP‐AlF 4 and S1‐ADP‐BeF x complexes represent structural analogues of different transition states of the ATPase cycle, namely the intermediate states S1 ** ‐ADP‐P i and S1 * ‐ATP, respectively.