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J. Biol. Chem., Vol. 264, Issue 1, 100-107, Jan, 1989
QH Gibson, JB Wittenberg, BA Wittenberg, D Bogusz and CA Appleby
The rates of reaction of oxygen, carbon monoxide, and nitric oxide with 14
plant hemoglobins have been determined by relaxation and stopped- flow
methods. The combination rates for oxygen lie between 0.12 and 0.26 x
10(9)/M.s, for carbon monoxide between 0.01 and 0.07 x 10(9)/M.s, and for
nitric oxide between 0.12 and 0.25 x 10(9)/M.s. The dissociation velocities
for oxygen range from 5 to 25/s, and for CO from 0.005 to 0.011 s. The
oxygen dissociation constants range only from 36 to 78 nM. Nanosecond
relaxation experiments show large differences between the proteins. Five
have known primary structures which correlate closely with the nanosecond
relaxations and less immediately with the millisecond reactions. The
relevant amino acid substitutions are concentrated in the C-E interhelical
region.
The kinetics of ligand binding to plant hemoglobins. Structural implications
Department of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
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