ESR studies of heat denaturation in Cu myoglobin complexes

An investigation is made on the behaviour of Cu2+ and Fe3+ in copper doped myoglobin, subjected to heat treatment. ESR is observed at X-band. The amplitude of the g = 5.9 line of the high spin F3+ in met-myoglobin is studied as a function of the temperature of the heat treatment, the pH and the length of time of exposure to the heat treatment. These experiments are performed for both the pure protein and for the copper-myoglobin complex, at pH between 5 and 8.5. Results concerning the decrease of the amplitude of Fe3+ high spin signal are discussed in comparison with Hollocher's results in hemoglobin. The Cu spectra obtained are interpreted, with the aid of a computer program, Kivelson and Neiman's results being used to analyse the authors data