Abstract
Electron paramagnetic resonance was used to follow the time dependence of heat denaturation of met- and nitrosyl-haemoglobin (metHb and HbNO) at 60°C, 70°C and 80°C. The spectral changes of both complexes indicate that conformational changes in the protein manifest themselves in changes of the equilibrium of hemichromes in metHb and of six- and five-coordinated iron in HbNO. The formation of a hemichrome which has not been described before, with g=2.45, 2.27 and 1.85, is observed. A HisFeCys complex is proposed for its structure
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