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The FeIV 2(μ-O)2 cluster and bridge O2 activation at the active center of methane monooxygenase

  • Chemistry of Natural Compounds and Bioorganic Chemistry
  • Published:
Russian Chemical Bulletin Aims and scope

Abstract

The newest experimental data concerning soluble forms of methane monooxygenase (MMO) were analyzed taking into account the bridge mechanism of O2 activation by this enzyme proposed earlier. The results confirm that the scheme suggested and the structures of the key intermediates are valid and show a basic difference between the mechanisms of activation for heme (cytochrome P-450) and non-heme (MMO) monooxygenases. The X-ray diffraction analysis of MMO allowed us to develop a more detailed scheme that reflects the dynamics of O2 activation and the role of ligands in this process.

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Authors and Affiliations

  1. Institute of Chemical Physics in Chernogolovka, Russian Academy of Sciences, 142432, Chernogolovka, Moscow Region, Russian Federation

    A. A. Shteinman

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  1. A. A. Shteinman
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Translated fromIzvestiya Akademii Nauk. Seriya Khimicheskaya, No. 9, pp. 1676–1682, September, 1997.

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Shteinman, A.A. The FeIV 2(μ-O)2 cluster and bridge O2 activation at the active center of methane monooxygenase. Russ Chem Bull 46, 1599–1605 (1997). https://doi.org/10.1007/BF02502948

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  • DOI: https://doi.org/10.1007/BF02502948

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