Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29-->Tyr sperm whale myoglobin mutant.

The kinetics of binding of O2, CO, and NO to the octameric, two-domain hemoglobins of the parasitic nematodes Pseudoterranova decipiens and Ascaris suum were determined on nanosecond and picosecond time scales using flash photolysis. The two nematode hemoglobins have very similar kinetic properties. On the picosecond time scale, they exhibit an unusual behavior in showing a geminate reaction with oxygen that is biphasic and dependent on the flash intensity. The geminate reaction with NO is also faster and more complete than for sperm whale myoglobin; however, in contrast to the O2 reaction, it is homogeneous. In addition, the oxygen dissociation rate of P. decipiens hemoglobin, 0.0035 s-1, is as low as that of A. suum hemoglobin, 0.004 s-1 (Gibson, Q. H., and Smith, M. H. (1965) Proc. R. Soc. Lond. B Biol. Sci. 163, 206-214). A mutant of sperm whale myoglobin suggested by sequence alignment of the nematode hemoglobins, Leu-29-->Tyr, did not have kinetic properties similar to them.