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Science 16 February 1990:
Vol. 247. no. 4944, pp. 831 - 833
DOI: 10.1126/science.2154849
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Articles

Science, Vol 247, Issue 4944, 831-833
Copyright © 1990 by American Association for the Advancement of Science

articles

NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex

AM Burch, SE Rigby, WD Funk, RT MacGillivray, MR Mauk, AG Mauk, and GR Moore

School of Chemical Sciences, University of East Anglia, Norwich, United Kingdom.

The complex formed in solution by native and chemically modified cytochrome c with cytochrome b5 has been studied by 1H and 13C nuclear magnetic resonance spectroscopy (NMR). Contrary to predictions of recent theoretical analysis, 1H NMR spectroscopy indicates that there is no major movement of cytochrome c residue Phe82 on binding to cytochrome b5. The greater resolution provided by 13C NMR spectroscopy permits detection of small perturbations in the environments of cytochrome c residues Ile75 and Ile85 on binding with cytochrome b5, a result that is in agreement with earlier model-building experiments. As individual cytochrome c lysyl residues are resolved in the 1H NMR spectrum of N-acetimidylated cytochrome c, the interaction of this modified protein with cytochrome b5 has been studied to evaluate the number of cytochrome c lysyl residues involved in binding to cytochrome b5. The results of this experiment indicate that at least six lysyl residues are involved, two more than predicted by static model building, which indicates that cytochrome c and cytochrome b5 form two or more structurally similar 1:1 complexes in solution.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Cloning, Overexpression in Escherichia coli, Structural and Functional Characterization of House Fly Cytochrome b5.
V. M. Guzov, H. L. Houston, M. B. Murataliev, F. A. Walker, and R. Feyereisen (1996)
J. Biol. Chem. 271, 26637-26645
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