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J Biol Chem, Vol. 274, Issue 16, 11383-11389, April 16, 1999

The Structure of an Electron Transfer Complex Containing a Cytochrome c and a Peroxidase

Graham W. Pettigrew, Susana Prazeres^¶, Cristina Costa^¶, Nuno Palma^¶, Ludwig Krippahl^¶, Isabel Moura^¶, and Jose J. G. Moura^¶

From the  Department of Preclinical Veterinary studies, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Summerhall Edinburgh EH9 1QH, United Kingdom, the ^¶ Departamento de Quimica, Centro de Quimica Fina e Biotecnologia, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2825 Monte de Caparica, Portugal, and the  Instituto Superior de Ciencias da Saude, Quinta da Granja, 2825 Monte de Caparica, Portugal

Efficient biological electron transfer may require a fluid association of redox partners. Two noncrystallographic methods (a new molecular docking program and ¹H NMR spectroscopy) have been used to study the electron transfer complex formed between the cytochrome c peroxidase (CCP) of Paracoccus denitrificans and cytochromes c. For the natural redox partner, cytochrome c₅₅₀, the results are consistent with a complex in which the heme of a single cytochrome lies above the exposed electron-transferring heme of the peroxidase. In contrast, two molecules of the nonphysiological but kinetically competent horse cytochrome bind between the two hemes of the peroxidase. These dramatically different patterns are consistent with a redox active surface on the peroxidase that may accommodate more than one cytochrome and allow lateral mobility.

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