Structures of the Apo and FAD-Bound Forms of 2-Hydroxybiphenyl 3-monooxygenase (HbpA) Locate Activity Hotspots Identified by Using Directed Evolution

Jensen, Chantel N., Mielke, Tamara, Farrugia, Joseph E. et al. (5 more authors) (2015) Structures of the Apo and FAD-Bound Forms of 2-Hydroxybiphenyl 3-monooxygenase (HbpA) Locate Activity Hotspots Identified by Using Directed Evolution. Chembiochem. 968–976. ISSN 1439-7633

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Copyright, Publisher and Additional Information: © 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Keywords: biotransformations, FAD, flavoprotein, hydroxylation, monooxygenases
Dates:
  • Published: 13 April 2015
Institution: The University of York
Academic Units: The University of York > Faculty of Sciences (York) > Chemistry (York)
Depositing User: Pure (York)
Date Deposited: 21 Jul 2015 11:50
Last Modified: 04 Feb 2024 00:35
Published Version: https://doi.org/10.1002/cbic.201402701
Status: Published
Refereed: Yes
Identification Number: https://doi.org/10.1002/cbic.201402701
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Description: Structures of the Apo and FAD-Bound Forms of2-Hydroxybiphenyl 3-monooxygenase (HbpA) LocateActivity Hotspots Identified by Using Directed Evolution

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