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Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)

COVER PICTURE: Thomas Reiner, Dominik Jantke, Alexander N. Marziale, Andreas Raba, and Jörg Eppinger* The cover picture illustrates the concept of using metal-conjugated affinity labels (m-ALs) to convert proteases into well-defined and catalytically active artificial metalloenzymes. The X-ray struc...

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Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646424/
http://dx.doi.org/10.1002/open.201390005
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collection PubMed
description COVER PICTURE: Thomas Reiner, Dominik Jantke, Alexander N. Marziale, Andreas Raba, and Jörg Eppinger* The cover picture illustrates the concept of using metal-conjugated affinity labels (m-ALs) to convert proteases into well-defined and catalytically active artificial metalloenzymes. The X-ray structure of the papain-bound inhibitor E64c (orange) served as the basis to predict the orientation of the half-sandwich rhodium(III) moiety (yellow sphere) within the binding pocket of the protease. The well-defined position of the affinity label on the protein surface leads to a distinct environment of the metal center, which translates into enantiomeric ratios of up to 82:18 in the aqueous hydrogenation of ketones. For more details, see the Communication by Jörg Eppinger et al., on p. 50 ff. [Image: see text]
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spelling pubmed-36464242014-02-18 Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013) ChemistryOpen Cover Picture COVER PICTURE: Thomas Reiner, Dominik Jantke, Alexander N. Marziale, Andreas Raba, and Jörg Eppinger* The cover picture illustrates the concept of using metal-conjugated affinity labels (m-ALs) to convert proteases into well-defined and catalytically active artificial metalloenzymes. The X-ray structure of the papain-bound inhibitor E64c (orange) served as the basis to predict the orientation of the half-sandwich rhodium(III) moiety (yellow sphere) within the binding pocket of the protease. The well-defined position of the affinity label on the protein surface leads to a distinct environment of the metal center, which translates into enantiomeric ratios of up to 82:18 in the aqueous hydrogenation of ketones. For more details, see the Communication by Jörg Eppinger et al., on p. 50 ff. [Image: see text] WILEY-VCH Verlag 2013-04 2013-04-23 /pmc/articles/PMC3646424/ http://dx.doi.org/10.1002/open.201390005 Text en Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Cover Picture
Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title_full Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title_fullStr Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title_full_unstemmed Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title_short Cover Picture: Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes (ChemistryOpen 2/2013)
title_sort cover picture: metal-conjugated affinity labels: a new concept to create enantioselective artificial metalloenzymes (chemistryopen 2/2013)
topic Cover Picture
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646424/
http://dx.doi.org/10.1002/open.201390005