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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
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).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/301169a0
This article is cited by
-
The sequence homologies of cytochromes P-450 and active-site geometries
Journal of Computer-Aided Molecular Design (1992)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.