J. Vanderkooi, K. Sharp, J. Fidy
Aug 17, 1994
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Abstract
Mesoporphyrin IX was used as a fluorescent analogue of heme in cytochrome c peroxidase (CcP). Details of the fluorescence spectra of CcP obtained under conditions of energy selection revealed interactions of the porphyrin with the heme pocket. It was shown that the energy of a 0,0 transition shifted with pH in parallel with changes in the electric field of the protein.