THE DEPENDENCE OF THE QUANTUM YIELD OF LIGAND PHOTODISSOCIATION FROM HAEM PROTEINS ON ULTRAFAST RECOMBINATION

Abstract— Measurements of relative photolysis yields in nanosecond flash photolysis studies of carbon monoxide and dioxygen complexes of haemoglobin and myoglobin are compared with published values of the quantum efficiency for photodissociation obtained from microsecond flash or continuous photolysis studies. It is shown that the differences in quantum yield between HbCO and MbCO and between Hb02 and Mb02 can be correlated with the different extent of ultrafast recombination observed in the nanosecond experiments. Furthermore, the temperature dependence of the quantum yield in the case of HbCO can be entirely attributed to the effect of temperature on the ultrafast recombination.

[1]  Q. Gibson,et al.  Photosensitivity of Hæm Compounds , 1957, Nature.

[2]  Q. Gibson The photochemical formation of a quickly reacting form of haemoglobin. , 1959, The Biochemical journal.

[3]  E. Antonini,et al.  Studies on the relations between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin. , 1961, The Journal of biological chemistry.

[4]  M. Brunori,et al.  Studies on the quantum yields of the photodissociation of carbon monoxide from hemoglobin and myoglobin. , 1967, Biochemistry.

[5]  R. Benesch,et al.  Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. , 1968, Proceedings of the National Academy of Sciences of the United States of America.

[6]  L. Lindqvist,et al.  Rapid structural changes in human hemoglobin studied by laser photolysis. , 1972, Biochemical and biophysical research communications.

[7]  M. Brunori,et al.  Carbon monoxide binding by simple heme proteins under photodissociating conditions. , 1973, Biochemistry.

[8]  M. Brunori,et al.  Heme proteins: quantum yield determined by the pulse method. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[9]  P. Phillipson,et al.  Heme proteins: effect of an intermediate on photochemical behavior. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[10]  B Alpert,et al.  The kinetics of conformational changes in hemoglobin, studied by laser photolysis. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[11]  H Frauenfelder,et al.  Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.

[12]  Q. Gibson,et al.  Photodissociation of ligands from heme and heme proteins. Effect of temperature and organic phosphate. , 1977, The Journal of biological chemistry.

[13]  Q. Gibson,et al.  On the photosensitivity of liganded hemoproteins and their metal-substituted analogues. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[14]  M. Perutz,et al.  Binding of carbon monoxide to isolated hemoglobin chains. , 1978, Biochemistry.

[15]  P. Rentzepis,et al.  Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[16]  R. Morris,et al.  Ultra-fast recombination in nanosecond laser photolysis of carbonylhaemoglobin , 1979 .

[17]  L. Lindqvist,et al.  Transient effects in the nanosecond laser photolysis of carboxyhemoglobin , 1979 .