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Insights into the active site of the plant alternative oxidase and its relationship to function

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Regulation of Primary Metabolic Pathways in Plants

Part of the book series: Proceedings of the Phytochemical Society of Europe ((PPSE,volume 42))

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Abstract

This review is focused upon our current understanding of the structure and function of the mitochondrial alternative oxidase. Molecular modelling techniques have been used to model the active site of the alternative oxidase using the 3D-coordinates of known di-iron carboxylate proteins (methane monooxygenase and ribonucleotide reductase). Results are discussed in terms of how the proposed structure of the alternative oxidase relates to its postulated function as a di-oxygen scavenger.

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Authors and Affiliations

  1. Biochemistry Department, School of Biological Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK

    Charles Affourtit & Anthony L. Mooore

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  1. Charles Affourtit
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  2. Anthony L. Mooore
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Editors and Affiliations

  1. Department of Plant Sciences, University of Oxford, Oxford, UK

    Nicholas J. Kruger , Steven A. Hill  & R. George Ratcliffe ,  & 

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Affourtit, C., Mooore, A.L. (1999). Insights into the active site of the plant alternative oxidase and its relationship to function. In: Kruger, N.J., Hill, S.A., Ratcliffe, R.G. (eds) Regulation of Primary Metabolic Pathways in Plants. Proceedings of the Phytochemical Society of Europe, vol 42. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4818-4_2

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  • DOI: https://doi.org/10.1007/978-94-011-4818-4_2

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6021-9

  • Online ISBN: 978-94-011-4818-4

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