-transparent.png){kind=logo}
The time course of oxygen-18 exchange between [18O]Pi and normal water, catalyzed by myosin subfragment 1 in the presence of MgADP, was followed using the shift in 31P NMR caused by the presence of oxygen-18 bound to the phosphorus. Essentially all molecules of [18O]Pi that bind to the enzyme undergo complete exchange and are released as [16O4]Pi. Exchange probably occurs by formation of myosin.ATP from a myosin.ADP.Pi complex and is rapid relative to release of Pi from this complex. The kinetics of exchange give a value for the rate constant for binding Pi to myosin.ADP of 0.23 M-1 S-1 (pH 8.0, 22 degrees C). This value is consistent with exchange occurring by reversal of the ATP-ase reaction back to the myosin.ATP complex.
M R Webb, and
G G McDonald, and
D R Trentham
January 1978,
Proceedings of the National Academy of Sciences of the United States of America,
M R Webb, and
G G McDonald, and
D R Trentham
June 1978,
The Journal of biological chemistry,
M R Webb, and
G G McDonald, and
D R Trentham
January 1982,
Advances in myocardiology,
M R Webb, and
G G McDonald, and
D R Trentham
August 1976,
Biokhimiia (Moscow, Russia),
M R Webb, and
G G McDonald, and
D R Trentham
January 1990,
The Journal of biological chemistry,
M R Webb, and
G G McDonald, and
D R Trentham
January 1977,
Acta biochimica et biophysica; Academiae Scientiarum Hungaricae,
M R Webb, and
G G McDonald, and
D R Trentham
December 1984,
Biochemistry,
M R Webb, and
G G McDonald, and
D R Trentham
April 1980,
Biochemistry,
M R Webb, and
G G McDonald, and
D R Trentham
April 1973,
Archives of biochemistry and biophysics,
M R Webb, and
G G McDonald, and
D R Trentham
May 1967,
Tsitologiia,
