Abstract
Various studies have shown that reaction rates between revers-ibly binding electron transfer proteins depend strongly on solution ionic strength1–7. These observations suggest that inter-molecular electrostatic interactions are important in facilitating the formation of a productive reaction complex. A recently examined system involves the reduction of vertebrate cytochrome c by bacterial flavodoxin8,9. Although this is a non-physiological reaction, it proceeds with rates typical for natural partners and is similarly inhibited at high ionic strengths. Here we describe computational studies which examine the role of electrostatics in the formation of a putative reaction complex between flavodoxin and cytochrome c. The results suggest that electrostatic interactions preorient the molecules before they make physical contact, facilitating the formation of an optimal reaction complex.
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References
Smith, H. T., Ahmed, A. J. & Millett, F. J. biol. Chem. 256, 4984–4990 (1981).
Geren, L. M. & Millett, F. J. biol. Chem. 256, 4851–4855 (1981).
Foust, G. P., Mayhew, S. G. & Massey, V. J. biol. Chem. 244, 964–970 (1969).
Batie, C. J. & Kamin, H. J. biol. Chem. 256, 7756–7763 (1981).
Gacon, G., Lostanlen, D., Labie, D. & Kaplan, J. Proc. natn. Acad. Sci. U.S.A. 77, 1917–1921 (1980).
Kuma, F. J. biol. Chem. 256, 5518–5523 (1981).
Koppenol, W. H. & Margoliash, E. J. biol. Chem. 257, 4426–4437 (1982).
Simondsen, R. P., Weber, P. C., Salemme, F. R. & Tollin, G. Biochemistry (in the press).
Simondsen, R. P. & Tollin, G. in Flavins and Flavoproteins (eds Massey, V. & Williams, C. H.) 719–724 (Elsevier, New York, 1982).
Swanson, R. et al. J. biol. Chem. 252, 759–775 (1977).
Bernstein, F. G. et al. J. molec. Biol 112, 535–542 (1977).
Shire, S. J., Hanania, G. I. H. & Gurd, F. R. N. Biochemistry 13, 2967–2974 (1974).
Matthew, J. B., Hanania, G. H. I. & Gurd, F. R. N. Biochemistry 18, 1919–1928 (1979).
Matthew, J. B. & Richards, F. M. Biochemistry (in the press).
Salemme, F. R., Kraut, J. & Kamen, M. D. J. biol. Chem. 245, 7701–7716 (1973).
Salemme, F. R. A. Rev. Biochem. 46, 299–329 (1977).
Koppenol, W. H., Vroonland, C. A. J. & Braams, R. Biochim. biophys. Acta 503, 499–508 (1978).
Smith, W. W., Burnett, R. M., Darling, G. D. & Ludwig, M. L. J. molec. Biol. 117, 195–225 (1977).
Salemme, F. R. J. molec. Biol. 102, 563–568 (1977).
Poulos, T. L. & Kraut, J. J. biol. Chem. 10322–10330 (1980).
Ross, P. D. & Subramanian, S. Biochemistry 20, 3096–3102 (1981).
Chothia, C. & Janin, J. Nature 256, 705–707 (1975).
Winter, R. B., Berg, O. G. & Von Hippel, P. H. Biochemistry 20, 6861–6877 (1981).
Mauk, M. R., Reid, L. S. & Mauk, A. G. Biochemistry 21, 1843–1846 (1982).
Overfield, R. & Wraight, C. A. Biochemistry 19, 3322–3327, 3328–3334 (1980).
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Matthew, J., Weber, P., Salemme, F. et al. Electrostatic orientation during electron transfer between flavodoxin and cytochrome c. Nature 301, 169–171 (1983). https://doi.org/10.1038/301169a0
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DOI: https://doi.org/10.1038/301169a0
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