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J. Biol. Chem., Vol. 268, Issue 10, 6855-6857, 04, 1993
M Ikeda-Saito, Y Dou, T Yonetani, JS Olson, T Li, R Regan and QH Gibson
There are at least two picosecond kinetic components in the rebinding of NO
to native sperm whale myoglobin. Petrich et al. (Petrich, J. W., Lambry,
J.-C., Kuczera, K., Karplus, M., Poyart, C., and Martin, J.-L. (1991)
Biochemistry 30, 3975-3987) attribute the slowing of the reaction to a
movement of the iron atom out of the plane of the heme following ligand
dissociation. In contrast, Gibson et al. (Gibson, Q. H., Regan, R., Elber,
R., Olson, J. S., and Carver, T. E. (1992) J. Biol. Chem. 267, 22022-22034)
have explained multiphasic geminate reactions by diffusion of NO into the
distal heme pocket as determined by its detailed structure. O2 and NO
rebinding to iron and cobalt derivatives of native, V68F, and V68I sperm
whale myoglobin has been examined. Each iron protein shows a biphasic time
course of NO rebinding reactions with widely different rates and
amplitudes. Although cobalt does not move out of the plane of the porphyrin
on ligand removal, the reactions of the iron and cobalt derivatives of each
protein were closely similar. The time course of O2 rebinding to cobalt was
also similar to that of NO rebinding to iron. These results are consistent
with a primary role for the structure of the distal pocket in determining
diffusion of ligands away from the metal atom and as a result the time
course of picosecond ligand rebinding.
Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding
Department of Physiology and Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106-4970.
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