Electric field and conformational effects in cytochrome c peroxidase studied by high-resolution fluorescence spectroscopy and electrostatic calculations

Jane M. Vanderkooi; K. Sharp; J. Fidy; T. Yonetani; H. Anni

doi:10.1117/12.182744

17 August 1994 Electric field and conformational effects in cytochrome c peroxidase studied by high-resolution fluorescence spectroscopy and electrostatic calculations

Jane M. Vanderkooi, K. Sharp, J. Fidy, T. Yonetani, H. Anni

Author Affiliations +

Proceedings Volume 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV; (1994) https://doi.org/10.1117/12.182744
Event: OE/LASE '94, 1994, Los Angeles, CA, United States

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.

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Jane M. Vanderkooi, K. Sharp, J. Fidy, T. Yonetani, and H. Anni "Electric field and conformational effects in cytochrome c peroxidase studied by high-resolution fluorescence spectroscopy and electrostatic calculations", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182744

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