Abstract
A recent development in the field of heme proteins has been the engineering of cavity mutants in which the axial coordinating residue is replaced by a smaller, noncoordinating residue, leaving a cavity that can then be filled by exogenous ligands. In this manner, potential models for the cysteinate-ligated cytochrome P-450 monooxygenases have been prepared using the H93G cavity mutant of sperm whale myoglobin in which the coordinating histidine has been replaced by glycine. Magnetic circular dichroism (MCD) spectroscopy has been used for structural characterization of several ferric and ferrous thiolate-H93G adducts. Ferric mixed-ligand complexes can be prepared with neutral sixth ligands. The model breaks down in two cases: (i) when anionic ligands are added to the ferric-thiolate complex and (ii) on reduction of the ferric-thiolate complex. Results are discussed in the context of the H93C mutants of myoglobin and the stabilizing influences on the cytochrome P-450 heme-cysteinate complex.
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