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Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site

Since the discovery of the biological relevance of rare earth elements (REEs) for numerous different bacteria, questions concerning the advantages of REEs in the active sites of methanol dehydrogenases (MDHs) over calcium(II) and of why bacteria prefer light REEs have been a subject of debate. Here...

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Autores principales: Jahn, Bérénice, Pol, Arjan, Lumpe, Henning, Barends, Thomas R. M., Dietl, Andreas, Hogendoorn, Carmen, Op den Camp, Huub J. M., Daumann, Lena J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100108/
https://www.ncbi.nlm.nih.gov/pubmed/29524328
http://dx.doi.org/10.1002/cbic.201800130
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author Jahn, Bérénice
Pol, Arjan
Lumpe, Henning
Barends, Thomas R. M.
Dietl, Andreas
Hogendoorn, Carmen
Op den Camp, Huub J. M.
Daumann, Lena J.
author_facet Jahn, Bérénice
Pol, Arjan
Lumpe, Henning
Barends, Thomas R. M.
Dietl, Andreas
Hogendoorn, Carmen
Op den Camp, Huub J. M.
Daumann, Lena J.
author_sort Jahn, Bérénice
collection PubMed
description Since the discovery of the biological relevance of rare earth elements (REEs) for numerous different bacteria, questions concerning the advantages of REEs in the active sites of methanol dehydrogenases (MDHs) over calcium(II) and of why bacteria prefer light REEs have been a subject of debate. Here we report the cultivation and purification of the strictly REE‐dependent methanotrophic bacterium Methylacidiphilum fumariolicum SolV with europium(III), as well as structural and kinetic analyses of the first methanol dehydrogenase incorporating Eu in the active site. Crystal structure determination of the Eu‐MDH demonstrated that overall no major structural changes were induced by conversion to this REE. Circular dichroism (CD) measurements were used to determine optimal conditions for kinetic assays, whereas inductively coupled plasma mass spectrometry (ICP‐MS) showed 70 % incorporation of Eu in the enzyme. Our studies explain why bacterial growth of SolV in the presence of Eu(3+) is significantly slower than in the presence of La(3+)/Ce(3+)/Pr(3+): Eu‐MDH possesses a decreased catalytic efficiency. Although REEs have similar properties, the differences in ionic radii and coordination numbers across the series significantly impact MDH efficiency.
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spelling pubmed-61001082018-08-27 Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site Jahn, Bérénice Pol, Arjan Lumpe, Henning Barends, Thomas R. M. Dietl, Andreas Hogendoorn, Carmen Op den Camp, Huub J. M. Daumann, Lena J. Chembiochem Full Papers Since the discovery of the biological relevance of rare earth elements (REEs) for numerous different bacteria, questions concerning the advantages of REEs in the active sites of methanol dehydrogenases (MDHs) over calcium(II) and of why bacteria prefer light REEs have been a subject of debate. Here we report the cultivation and purification of the strictly REE‐dependent methanotrophic bacterium Methylacidiphilum fumariolicum SolV with europium(III), as well as structural and kinetic analyses of the first methanol dehydrogenase incorporating Eu in the active site. Crystal structure determination of the Eu‐MDH demonstrated that overall no major structural changes were induced by conversion to this REE. Circular dichroism (CD) measurements were used to determine optimal conditions for kinetic assays, whereas inductively coupled plasma mass spectrometry (ICP‐MS) showed 70 % incorporation of Eu in the enzyme. Our studies explain why bacterial growth of SolV in the presence of Eu(3+) is significantly slower than in the presence of La(3+)/Ce(3+)/Pr(3+): Eu‐MDH possesses a decreased catalytic efficiency. Although REEs have similar properties, the differences in ionic radii and coordination numbers across the series significantly impact MDH efficiency. John Wiley and Sons Inc. 2018-04-16 2018-06-04 /pmc/articles/PMC6100108/ /pubmed/29524328 http://dx.doi.org/10.1002/cbic.201800130 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Full Papers
Jahn, Bérénice
Pol, Arjan
Lumpe, Henning
Barends, Thomas R. M.
Dietl, Andreas
Hogendoorn, Carmen
Op den Camp, Huub J. M.
Daumann, Lena J.
Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title_full Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title_fullStr Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title_full_unstemmed Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title_short Similar but Not the Same: First Kinetic and Structural Analyses of a Methanol Dehydrogenase Containing a Europium Ion in the Active Site
title_sort similar but not the same: first kinetic and structural analyses of a methanol dehydrogenase containing a europium ion in the active site
topic Full Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6100108/
https://www.ncbi.nlm.nih.gov/pubmed/29524328
http://dx.doi.org/10.1002/cbic.201800130
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