Magnetic circular dichroism in hemoglobin

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Abstract
Magnetic circular dichroism (MCD) and absorption have been measured in various derivatives of hemoglobin in an applied field of 16 kG at temperatures ranging from 77 to 294 °K. The visible and Soret bands have been studied. We develop a spin–orbit coupling model to help explain the sign, magnitude, and 1/T temperature dependence of the MCD of deoxyhemoglobin. The results for deoxyhemoglobin are compared with those for unligated separated alpha and beta chains. Differences in spectra occur which can only be attributed to the different temperature dependent heme environments for chains and for tetramers. Cyanomethemoglobin and oxyhemoglobin are also discussed.