Structure–function relationships of anaerobic gas-processing metalloenzymes

Juan C. Fontecilla-Camps, Patricia Amara, Christine Cavazza, Yvain Nicolet and Anne Volbeda
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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

Nature, 2009, vol. 460, issue 7257, 814-822

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08299

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