-transparent.png){kind=logo}
The effects of chloride ion concentration on the rate constants for association of carbon monoxide with human hemoglobin A and a synthetic form of the mutant hemoglobin Rothschild (beta 37 Trp-->Arg) have been investigated by stopped-flow techniques. Previous studies of the structure [Kavanaugh et al. (1992) Biochemistry 31, 4111] and functional properties [Rivetti et al. (1993) Biochemistry 32, 2888] of hemoglobin Rothschild crystallized in the T state have demonstrated that the mutant arginine residues create new chloride ion binding sites and that chloride ions act to lower the oxygen affinity of hemoglobin Rothschild in these crystals. The studies reported here demonstrate a parallel effect of chloride ions on the rate of CO association with deoxygenated hemoglobin Rothschild in solution. Although the kinetics of CO binding to this hemoglobin in solution exhibit a Bohr effect, the chloride effect is independent of pH. In addition, we find that other halide ions have similar effects on the rate constants for the association of CO with this hemoglobin variant.
R M Kelly, and
H L Hui, and
R W Noble
December 1980,
Journal of molecular biology,
R M Kelly, and
H L Hui, and
R W Noble
June 1993,
Biochemistry,
R M Kelly, and
H L Hui, and
R W Noble
January 1982,
Hemoglobin,
R M Kelly, and
H L Hui, and
R W Noble
April 1992,
Biochemistry,
R M Kelly, and
H L Hui, and
R W Noble
October 1977,
FEBS letters,
R M Kelly, and
H L Hui, and
R W Noble
August 1981,
Archives of biochemistry and biophysics,
R M Kelly, and
H L Hui, and
R W Noble
June 1984,
The Journal of clinical investigation,
R M Kelly, and
H L Hui, and
R W Noble
September 1983,
Biochimica et biophysica acta,
R M Kelly, and
H L Hui, and
R W Noble
January 1987,
Nouvelle revue francaise d'hematologie,
R M Kelly, and
H L Hui, and
R W Noble
January 1988,
Hemoglobin,
