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Structural dynamics in an electron–transfer complex

Nature Structural Biology volume 1, pages 234–238 (1994)Cite this article

Abstract

The dynamic behaviour of the complex of horse cytochrome c with cytochrome c peroxidase, an electron–transfer complex, was studied in solution by a hydrogen exchange labelling method together with two–dimensional NMR analysis. Although cytochrome c hydrogens in the expected binding region exhibit slowed exchange, the measured slowing factors are very small, indicating that hydrogen–exchange occurs with little hindrance from within the binding interface. The complex in solution must therefore be highly mobile rather than rigidly defined, as implied by the crystalline complex. This result is in conflict with the concept that biological electron transfer occurs by way of predetermined covalent pathways.

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Authors and Affiliations

  1. Johnson Research Foundation, Department of Biochemistry & Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, 19104-6059, USA

    Mei-Fen Jeng & S. Walter Englander

  2. Department of Chemistry, University of Rochester, Rochester, New York, 14627, USA

    Kelli Pardue, Jill Short Rogalskyj & George McLendon

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  1. Mei-Fen Jeng
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  4. Jill Short Rogalskyj
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Jeng, MF., Englander, S., Pardue, K. et al. Structural dynamics in an electron–transfer complex. Nat Struct Mol Biol 1, 234–238 (1994). https://doi.org/10.1038/nsb0494-234

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