Characterization of the Covalently Bound Anionic Flavin Radical in Monoamine Oxidase A by Electron Paramagnetic Resonance-Reference-Cited by-同舟云学术

Characterization of the Covalently Bound Anionic Flavin Radical in Monoamine Oxidase A by Electron Paramagnetic Resonance

Published:2007-11-29 Issue:51 Volume:129 Page:16091-16097
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kay Christopher W. M.¹,El Mkami Hassane¹,Molla Gianluca¹,Pollegioni Loredano¹,Ramsay Rona R.¹

Affiliation:

1. Contribution from the Department of Biology, University College London, Gower Street, London WC1E 6BT, U.K., Centre for Biomolecular Sciences and Department of Physics and Astronomy, University of St. Andrews, North Haugh, Saint Andrews, Fife KY16 9ST, U.K., and Department of Biotechnology and Molecular Sciences, University of Insubria, 21100 Varese, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja076090q

Reference70 articles.

1. The Chemical and Biological Versatility of Riboflavin

2. Flavoenzymes: diverse catalysts with recurrent features

3. Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD

4. The Covalently-Bound Flavin of Hepatic Monoamine Oxidase. 1. Isolation and Sequence of a Flavin Peptide and Evidence for Binding at the 8alpha Position

5. Structure and Mechanism of Monoamine Oxidase

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