Abstract
Fe-porphyrin is a common heme cofactor in the active sites of proteins, and plays important roles in a variety of biochemical functions. However, the origin of the diverse functions of Fe-porphyrin still remains unclear. Recent studies have suggested the possible biological significance of heme distortion in proteins. This article presents a review of the recent computational studies of the distortion effects of heme, an Fe-porphyrin found in a biological active site. A procedure to quantitatively evaluate the structural distortions of Fe-porphyrin is presented. Statistical analyses of the effect of porphyrin distortion in heme proteins and systematic density functional calculations of the change in the redox potential with heme distortions along the normal modes, to elucidate the structure–function relationship of heme, will then be described.
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