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Long-range electron transfer within metal-substituted protein complexes

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Long-Range Electron Transfer in Biology

Part of the book series: Structure and Bonding ((STRUCTURE,volume 75))

Abstract

Substitution of a closed-shell metalloporphyrin (MP) within one partner of a protein-protein complex makes it possible to study long-range electron transfer (ET), including direct measurement of both photoinitiated and thermal ET between the MP and heme (FeP) groups. Mixed-metal [M, M] hemoglobin hybrids have a structure that is fixed and well-characterized, which permits us to explore the factors that control the ET process by judicious selection of both the heme ligands and the substituting metal ion. In contrast, complexes between MP-substituted cytochrome c peroxidase (MCcP) and cytochrome c (FeCc) are conformationally mobile and the photoinitiated redox cycle provides a tool with which to explore the interplay between conformational interconversion and ET. Through a combination of metal substitution and site-directed mutagenesis, we probe the interfacial regulation of these processes.

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Authors and Affiliations

  1. Department of Chemistry, Northwestern University, 60208-3113, Evanston, IL, USA

    Brian M. Hoffman, Michael J. Natan, Judith M. Nocek & Sten A. Wallin

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  1. Brian M. Hoffman
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  2. Michael J. Natan
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  3. Judith M. Nocek
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  4. Sten A. Wallin
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© 1991 Springer-Verlag

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Hoffman, B.M., Natan, M.J., Nocek, J.M., Wallin, S.A. (1991). Long-range electron transfer within metal-substituted protein complexes. In: Long-Range Electron Transfer in Biology. Structure and Bonding, vol 75. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-53260-9_3

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  • DOI: https://doi.org/10.1007/3-540-53260-9_3

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-53260-6

  • Online ISBN: 978-3-540-46792-2

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