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Biophys J, December 2001, p. 3090-3104, Vol. 81, No. 6
*Universita' di Modena e Reggio Emilia, Dipartimento di Chimica,
Via Campi, 183-41100 Modena, Italy; European
Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, D-69012
Heidelberg, Germany; and European Media Laboratory
(EML), Schloss-Wolfsbrunnenweg 33, D-69118 Heidelberg, Germany
The oxidation of cytochrome f by the soluble
cupredoxin plastocyanin is a central reaction in the photosynthetic
electron transfer chain of all oxygenic organisms. Here, two different computational approaches are used to gain new insights into the role of
molecular recognition and protein-protein association processes in this
redox reaction. First, a comparative analysis of the computed molecular
electrostatic potentials of seven single and multiple point mutants of
spinach plastocyanin (D42N, E43K, E43N, E43Q/D44N, E59K/E60Q,
E59K/E60Q/E43N, Q88E) and the wt protein was carried out. The
experimentally determined relative rates (k2) for the set of plastocyanin mutants are
found to correlate well (r2 = 0.90 
0.97) with the computed measure of the similarity of the
plastocyanin electrostatic potentials. Second, the effects on the
plastocyanin/cytochrome f association rate of these mutations in the
plastocyanin "eastern site" were evaluated by simulating the
association of the wild type and mutant plastocyanins with cytochrome f
by Brownian dynamics. Good agreement between the computed and
experimental relative rates (k2)
(r2 = 0.89 0.92) was achieved
for the plastocyanin mutants. The results obtained by applying both
computational techniques provide support for the fundamental role of
the acidic residues at the plastocyanin eastern site in the association
with cytochrome f and in the overall electron-transfer process.
Biophys J, December 2001, p. 3090-3104, Vol. 81, No. 6
© 2001 by the Biophysical Society 0006-3495/01/12/3090/15 $2.00
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