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Proceedings Paper

Electric field and conformational effects in cytochrome c peroxidase studied by high-resolution fluorescence spectroscopy and electrostatic calculations
Author(s): Jane M. Vanderkooi; K. Sharp; J. Fidy; T. Yonetani; H. Anni
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Paper 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.

Paper Details

Date Published: 17 August 1994
PDF: 7 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182744
Show Author Affiliations
Jane M. Vanderkooi, Univ. of Pennsylvania School of Medicine (United States)
K. Sharp, Univ. of Pennsylvania School of Medicine (United States)
J. Fidy, Semmelweis Medical Univ. (Hungary)
T. Yonetani, Univ. of Pennsylvania School of Medicine (United States)
H. Anni, Univ. of Pennsylvania School of Medicine (United States)


Published in SPIE Proceedings Vol. 2137:
Time-Resolved Laser Spectroscopy in Biochemistry IV
Joseph R. Lakowicz, Editor(s)

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