Abstract
Oxyhemoglobin photolysis has been investigated with picosecond laser techniques. Transient light absorption changes observed within 500–600 nm reveal two processes following photodissociation: electronic relaxation up to 400 ps after dissociation and a partial religation during 3 ns. The kinetics of oxygen geminate recombination at pH 7 and 22°C has a monoexponential decay with a lifetime of 1.5 ns ± 0.1 ns.
Highlights
A number of nano-’2 and picosecond[3,4] photolysis investigations have been used to describe the dynamics of hemoglobin smctural adjustments by following the binding kinetics of the sixth axial ligand (CO or 02)
Recent experiments indicate that hemoglobin,[5] like a large number of other protein studied,[6] has rapid structural fluctuations that permit the penetration of oxygen molecules into the protein matrix
We demonstrate that picosecond photodissociation experiments provide information on oxygen recombination only if the kinetic evolution is followed at a wavelength where the absorption change due to these relaxation processes is low
Summary
A number of nano-’2 and picosecond[3,4] photolysis investigations have been used to describe the dynamics of hemoglobin smctural adjustments by following the binding kinetics of the sixth axial ligand (CO or 02). Recent experiments indicate that hemoglobin,[5] like a large number of other protein studied,[6] has rapid structural fluctuations that permit the penetration of oxygen molecules into the protein matrix. These studies generate a new Address reprint requests to: B. Laboratoire de Biologie Physicochimique, UER de Biochimie de Pads VII, Tour 42-43, 2, Place Jussieu, 75251 PARIS CEDEX 05, France.
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