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Structure–function relationships of anaerobic gas-processing metalloenzymes

Author

Listed:
  • Juan C. Fontecilla-Camps

    (Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'J.P. Ebel', CEA, CNRS, Université Joseph Fourier)

  • Patricia Amara

    (Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'J.P. Ebel', CEA, CNRS, Université Joseph Fourier)

  • Christine Cavazza

    (Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'J.P. Ebel', CEA, CNRS, Université Joseph Fourier)

  • Yvain Nicolet

    (Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'J.P. Ebel', CEA, CNRS, Université Joseph Fourier)

  • Anne Volbeda

    (Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'J.P. Ebel', CEA, CNRS, Université Joseph Fourier)

Abstract

Reactions involving H2, N2, CO, CO2 and CH4 are likely to have been central to the origin of life. This is indicated by the active-site structures of the enzymes involved, which are often reminiscent of minerals. Through the combined efforts of protein crystallography, various types of spectroscopy, theoretical calculations and model chemistry, it has been possible to put forward plausible mechanisms for gas-based metabolism by extant microorganisms. Although the reactions are based on metal centres, the protein matrix regulates reactivity and substrate and product trafficking through internal pathways, specific ligation and dielectricity.

Suggested Citation

  • Juan C. Fontecilla-Camps & Patricia Amara & Christine Cavazza & Yvain Nicolet & Anne Volbeda, 2009. "Structure–function relationships of anaerobic gas-processing metalloenzymes," Nature, Nature, vol. 460(7257), pages 814-822, August.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7257:d:10.1038_nature08299
    DOI: 10.1038/nature08299
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