A simple rapid-mixing technique is described which allows the recombination reaction between apomyoglobin and haemin to be studied within 0.3s of the splitting of myoglobin by dilute HCl. Evidence is presented that indicates that the recombination process occurs between folded ‘native’ apomyoglobin and monomeric haemin. Postulation of a one (or more)-intermediate recombination process, as suggested by other studies, is not necessary to explain the results. The effect, on the kinetics and mechanism of recombination, of the time of exposure to acid pH of the split myoglobin solution was investigated. The effect of temperature on the recombination kinetics was also studied.
