Geminate combination of oxygen with iron-cobalt hybrid hemoglobins.
Photodissociation of oxygen from the ferrous subunits of hybrid hemoglobins in which the heme of either the alpha or the beta chain has been replaced by cobalt protoporphyrin IX shows large differences between the subunits. With a 25-ns light pulse, the apparent quantum yield at the end of the flash is greater for the beta-iron hybrid than for the alpha-iron hybrid. With the beta-iron hybrid, the yield is greater when solution conditions favor the T-state. After the flash, a part of the oxygen which has been dissociated recombines with a half-time of the order of tens of nanoseconds. The proportion is greatest in the R-state at low temperature and least in the T-state. With the alpha-iron hybrid, oxygen is much less readily removed, and the rapid recombination is slight or absent. It is seen most clearly at low temperatures in conditions which favor the T-state. The long term (greater than 100 ns) effect is that oxygen is much more readily removed from the beta-iron hybrid in the T-state than under any other condition. Analogous flash experiments performed with human hemoglobin A may be closely simulated by superposition of the results obtained with the two hybrid hemoglobins under the same conditions. Isolated human alpha and beta--SH chains show differences similar to, but less marked than, those of the iron-cobalt hybrids.
D006454:Hemoglobins / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D010777:Photochemistry; D011166:Porphyrins / Q000378:metabolism*; D011524:Protoporphyrins / Q000378:metabolism*; D013997:Time Factors
D006454:Hemoglobins; D011166:Porphyrins; D011524:Protoporphyrins; C007095:cobaltiprotoporphyrin; D010100:Oxygen