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JBC, Vol. 252, Issue 22, 7955-7958, Nov, 1977
W. A. Saffran and Q. H. Gibson
The effect of temperature on ligand photodissociation from protoheme and
the heme proteins hemoglobin (Hb) and myoglobin (Mb) has been examined. The
quantum yield of photodissociation (phi) is greater at 40 degrees than at 0
degrees; in general, larger increases are seen in the less photosensitive
complexes, while phi does not change in the most photosensitive complexes.
The ratio of phi at 40 degrees to phi at 0 degrees is 1.8 for HbCO, 2.3 for
n-butyl isocyanide Hb, 2.7 for HbO2, and 1.3 for HbNO, with initial phi
values of 0.38, 0.26, 0.028, and 0.003, respectively. This pattern of
quantum yield increases is seen in protoheme as well as Hb and Mb ligand
photolysis. The allosteric effector inositol hexaphosphate increases the
quantum yield of lignad photolysis from hemoglobin. As with temperature,
inositol hexaphosphate addition has a larger effect on complexes of low
quantum yield; phi increases 1.2-fold for HbCO and 2.2-fold for HbO2 at 0
degrees. The results are discussed in terms of a model containing a
photoexcited intermediate (Phillipson, P.E., Ackerson, B.J., and Wyman, J.
(1973) Proc. Natl. Acad. Sci. U.S.A. 70, 1550-1553).
Photodissociation of ligands from heme and heme proteins. Effect of temperature and organic phosphate
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