1. Insights into the Proposed Copper–Oxygen Intermediates that Regulate the Mechanism of Reactions Catalyzed by Dopamine β-Monooxygenase, Peptidylglycine α-Hydroxylating Monooxygenase, and Tyramine β-Monooxygenase

  1. Kenneth D. Karlin3 and
  2. Shinobu Itoh4
  1. Robert L. Osborne1 and
  2. Judith P. Klinman2

Published Online: 11 AUG 2011

DOI: 10.1002/9781118094365.ch1

Copper-Oxygen Chemistry

Copper-Oxygen Chemistry

How to Cite

Osborne, R. L. and Klinman, J. P. (2011) Insights into the Proposed Copper–Oxygen Intermediates that Regulate the Mechanism of Reactions Catalyzed by Dopamine β-Monooxygenase, Peptidylglycine α-Hydroxylating Monooxygenase, and Tyramine β-Monooxygenase, in Copper-Oxygen Chemistry (eds K. D. Karlin and S. Itoh), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/9781118094365.ch1

Editor Information

  1. 3

    Department of Chemistry, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA

  2. 4

    Department of Material and Life Science, Division of Advanced Science and Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan

Author Information

  1. 1

    Department of Chemistry and California Institute for Quantitative Biosciences, University of California - Berkeley, Berkeley, CA 94720, USA

  2. 2

    Department of Chemistry, Department of Molecular and Cellular Biology, and California Institute for Quantitative Biosciences, University of California - Berkeley, Berkeley, CA 94720, USA

Publication History

  1. Published Online: 11 AUG 2011
  2. Published Print: 16 SEP 2011

ISBN Information

Print ISBN: 9780470528358

Online ISBN: 9781118094365

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Keywords:

  • copper–oxygen intermediates, regulating mechanism of reactions - catalyzed by dopamine β-monooxygenase, PHM and TbM;
  • oxidation–reduction reactions, for biological systems - reaction mechanisms, catalyzed by DbM, PHM and TbM;
  • enzyme mechanisms, derived from kinetic characterization - and kinetic isotope effects

Summary

This chapter contains sections titled:

  • General introduction

  • Comparative properties of dopamine β-monooxygenase (DβM), Peptidylglycine α-Hydroxylating Monooxygenase (PHM), and Tyramine β-Monooxygenase (TβM)

  • Sequence, structure, and spectroscopy

  • Enzyme mechanisms derived from kinetic characterization and kinetic isotope effects

  • A network of communication between CuM and CuH

  • Concluding remarks and future prospects

  • Abbreviations

  • References