Abstract
Abstract Reduced sulfmyoglobin has been shown to be in the ferrous state by optical titration with ferricyanide. The product of this reaction, ferric sulfmyoglobin, has been well characterized by electron paramagnetic resonance. The kinetics of autoxidation of ferrous sulfmyoglobin is reported. In the ferrous state, sulfmyoglobin has been shown to bind oxygen reversibly. It exhibits a rectangular hyperbolic binding curve (Hill coefficient n = 1.0) like that of myoglobin, but with a p½ at 5° and pH 8 of 0.7 atm or 530 mm Hg, corresponding to an oxygen affinity 2500-fold lower than that of myoglobin at the same temperature. This accounts for the apparent inability of sulfmyoglobin to bind O2 under physiological conditions. The low oxygen affinity is discussed in terms of structural features of the molecule which lower the electron density at the iron and is an example of electronic control of oxygen affinity in hemoglobin-like compounds.
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