Mechanisms for regulating electron transfer in multi-centre redox proteins

R Eryl Sharp, Stephen K Chapman

    Research output: Contribution to journalLiterature review

    44 Citations (Scopus)

    Abstract

    Protein-mediated electron transfer is a key process in nature. Many of the proteins involved in such electron transfers are complex and contain a number of redox-active cofactors. The very complexity of these multi-centre redox proteins has made it difficult to fully understand the various electron transfer events they catalyse. This is sometimes because the electron transfer steps themselves are gated or coupled to other processes such as proton transfer. However, with the molecular structures of many of these proteins now available it is possible to probe these electron transfer reactions at the molecular level. It is becoming apparent that many of these multi-centre redox proteins have rather subtle and elegant ways for regulating electron transfer. The purpose of this article is to illustrate how nature has used different approaches to control electron transfer in a number of different systems. Illustrative examples include: thermodynamic control of electron transfer in flavocytochromes b(2) and P450 BM3; a novel control mechanism involving calmodulin-binding-dependent electron transfer in neuronal nitric oxide synthase; the probable gating of electron transfer by ATP hydrolysis in nitrogenase; conformational gating of electron transfer in cytochrome cd(1); the regulation of electron transfer by protein dynamics in the cytochrome bc(1) complex; and finally the coupling of electron transfer to proton transfer in cytochrome c oxidase. (C) 1999 Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)143-158
    Number of pages16
    JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
    Volume1432
    Issue number2
    DOIs
    Publication statusPublished - 13 Jul 1999

    Keywords

    • BC(1) COMPLEX
    • AERUGINOSA NITRITE REDUCTASE
    • flavocytochrome b(2)
    • cytochrome cd(1)
    • MOLYBDENUM-IRON PROTEIN
    • electron transfer
    • redox proteins
    • cytochrome bc(1)
    • BOVINE HEART
    • cytochrome P450
    • nitric oxide synthase
    • CYTOCHROME-C-OXIDASE
    • AZOTOBACTER-VINELANDII
    • PROTON-TRANSFER
    • cytochrome c oxidase
    • RHODOBACTER-SPHAEROIDES
    • CEREVISIAE FLAVOCYTOCHROME B(2)
    • MOFE PROTEIN

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