Loading…
Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B
The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan gener...
Saved in:
| Published in: | Angewandte Chemie 2015-07, Vol.127 (31), p.9125-9128 |
|---|---|
| Main Authors: | , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3 |
| container_end_page | 9128 |
| container_issue | 31 |
| container_start_page | 9125 |
| container_title | Angewandte Chemie |
| container_volume | 127 |
| creator | Murray, Alexander T. Dowley, Myles J. H. Pradaux-Caggiano, Fabienne Baldansuren, Amgalanbaatar Fielding, Alistair J. Tuna, Floriana Hendon, Christopher H. Walsh, Aron Lloyd-Jones, Guy C. John, Matthew P. Carbery, David R. |
| description | The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan generates a catalyst system which facilitates biomimetic amine oxidation. Mechanistic and electron paramagnetic (EPR) spectroscopic data supports the conclusion that the reaction proceeds through a radical manifold. This data provides the first example of a biorelevant synthetic model for monoamine oxidase B activity.
MAO‐Nachahmer: Ein Modellflavin wird als Mimetikum der Monoaminoxidase B (MAO‐B) unter aeroben und Umgebungsbedingungen eingeführt. Kinetik‐ und EPR‐Studien geben Einblick in den Mechanismus: Ein geschwindigkeitsbestimmender Wasserstoffatomtransfer vom Amin zum Flavinakzeptor wird sowohl für das Modellsystem als auch für MAO‐B vorgeschlagen. |
| doi_str_mv | 10.1002/ange.201503654 |
| format | article |
| fullrecord | <record><control><sourceid>wiley_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1002_ange_201503654</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>ANGE201503654</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3</originalsourceid><addsrcrecordid>eNqFkLtOwzAUhi0EEqWwMucFUmwnvoQtjUoL9MLAZUGybMdGhjZBdhDNxsKL8iSkKipsTEc65_9-HX0AnCI4QBDiM1k9mQGGiMCEknQP9BDBKE4YYfugB2Gaxhyn2SE4CuEZQkgxy3rgsZCNXLaN01G-cpWJFmtXysbVVfRWlcZ3W-VM1US58bXqUkVdlW5zD-fRzK2c9m1U22hWV7X8LQjm6-NzeAwOrFwGc_Iz--DuYnRbTOLpYnxZ5NNYY8a7txKIMVSYYG4ws9JqTlGZKsg5wxnFKaaIKmJllihdUkYJV5YTQ5XVmpMy6YPBtlf7OgRvrHj1biV9KxAUGzdi40bs3HRAtgXe3dK0_6RFPh-P_rLxlnWhMesdK_2LoKyzLR7mY3F9fzO7KthQTJJvL3V4vQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B</title><source>Wiley-Blackwell Read & Publish Collection</source><creator>Murray, Alexander T. ; Dowley, Myles J. H. ; Pradaux-Caggiano, Fabienne ; Baldansuren, Amgalanbaatar ; Fielding, Alistair J. ; Tuna, Floriana ; Hendon, Christopher H. ; Walsh, Aron ; Lloyd-Jones, Guy C. ; John, Matthew P. ; Carbery, David R.</creator><creatorcontrib>Murray, Alexander T. ; Dowley, Myles J. H. ; Pradaux-Caggiano, Fabienne ; Baldansuren, Amgalanbaatar ; Fielding, Alistair J. ; Tuna, Floriana ; Hendon, Christopher H. ; Walsh, Aron ; Lloyd-Jones, Guy C. ; John, Matthew P. ; Carbery, David R.</creatorcontrib><description>The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan generates a catalyst system which facilitates biomimetic amine oxidation. Mechanistic and electron paramagnetic (EPR) spectroscopic data supports the conclusion that the reaction proceeds through a radical manifold. This data provides the first example of a biorelevant synthetic model for monoamine oxidase B activity.
MAO‐Nachahmer: Ein Modellflavin wird als Mimetikum der Monoaminoxidase B (MAO‐B) unter aeroben und Umgebungsbedingungen eingeführt. Kinetik‐ und EPR‐Studien geben Einblick in den Mechanismus: Ein geschwindigkeitsbestimmender Wasserstoffatomtransfer vom Amin zum Flavinakzeptor wird sowohl für das Modellsystem als auch für MAO‐B vorgeschlagen.</description><identifier>ISSN: 0044-8249</identifier><identifier>EISSN: 1521-3757</identifier><identifier>DOI: 10.1002/ange.201503654</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Amine ; Enzyme ; EPR-Spektroskopie ; Oxidation ; Reaktionsmechanismen</subject><ispartof>Angewandte Chemie, 2015-07, Vol.127 (31), p.9125-9128</ispartof><rights>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.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3</citedby><cites>FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Murray, Alexander T.</creatorcontrib><creatorcontrib>Dowley, Myles J. H.</creatorcontrib><creatorcontrib>Pradaux-Caggiano, Fabienne</creatorcontrib><creatorcontrib>Baldansuren, Amgalanbaatar</creatorcontrib><creatorcontrib>Fielding, Alistair J.</creatorcontrib><creatorcontrib>Tuna, Floriana</creatorcontrib><creatorcontrib>Hendon, Christopher H.</creatorcontrib><creatorcontrib>Walsh, Aron</creatorcontrib><creatorcontrib>Lloyd-Jones, Guy C.</creatorcontrib><creatorcontrib>John, Matthew P.</creatorcontrib><creatorcontrib>Carbery, David R.</creatorcontrib><title>Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B</title><title>Angewandte Chemie</title><addtitle>Angew. Chem</addtitle><description>The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan generates a catalyst system which facilitates biomimetic amine oxidation. Mechanistic and electron paramagnetic (EPR) spectroscopic data supports the conclusion that the reaction proceeds through a radical manifold. This data provides the first example of a biorelevant synthetic model for monoamine oxidase B activity.
MAO‐Nachahmer: Ein Modellflavin wird als Mimetikum der Monoaminoxidase B (MAO‐B) unter aeroben und Umgebungsbedingungen eingeführt. Kinetik‐ und EPR‐Studien geben Einblick in den Mechanismus: Ein geschwindigkeitsbestimmender Wasserstoffatomtransfer vom Amin zum Flavinakzeptor wird sowohl für das Modellsystem als auch für MAO‐B vorgeschlagen.</description><subject>Amine</subject><subject>Enzyme</subject><subject>EPR-Spektroskopie</subject><subject>Oxidation</subject><subject>Reaktionsmechanismen</subject><issn>0044-8249</issn><issn>1521-3757</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNqFkLtOwzAUhi0EEqWwMucFUmwnvoQtjUoL9MLAZUGybMdGhjZBdhDNxsKL8iSkKipsTEc65_9-HX0AnCI4QBDiM1k9mQGGiMCEknQP9BDBKE4YYfugB2Gaxhyn2SE4CuEZQkgxy3rgsZCNXLaN01G-cpWJFmtXysbVVfRWlcZ3W-VM1US58bXqUkVdlW5zD-fRzK2c9m1U22hWV7X8LQjm6-NzeAwOrFwGc_Iz--DuYnRbTOLpYnxZ5NNYY8a7txKIMVSYYG4ws9JqTlGZKsg5wxnFKaaIKmJllihdUkYJV5YTQ5XVmpMy6YPBtlf7OgRvrHj1biV9KxAUGzdi40bs3HRAtgXe3dK0_6RFPh-P_rLxlnWhMesdK_2LoKyzLR7mY3F9fzO7KthQTJJvL3V4vQ</recordid><startdate>20150727</startdate><enddate>20150727</enddate><creator>Murray, Alexander T.</creator><creator>Dowley, Myles J. H.</creator><creator>Pradaux-Caggiano, Fabienne</creator><creator>Baldansuren, Amgalanbaatar</creator><creator>Fielding, Alistair J.</creator><creator>Tuna, Floriana</creator><creator>Hendon, Christopher H.</creator><creator>Walsh, Aron</creator><creator>Lloyd-Jones, Guy C.</creator><creator>John, Matthew P.</creator><creator>Carbery, David R.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</scope><scope>24P</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20150727</creationdate><title>Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B</title><author>Murray, Alexander T. ; Dowley, Myles J. H. ; Pradaux-Caggiano, Fabienne ; Baldansuren, Amgalanbaatar ; Fielding, Alistair J. ; Tuna, Floriana ; Hendon, Christopher H. ; Walsh, Aron ; Lloyd-Jones, Guy C. ; John, Matthew P. ; Carbery, David R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amine</topic><topic>Enzyme</topic><topic>EPR-Spektroskopie</topic><topic>Oxidation</topic><topic>Reaktionsmechanismen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murray, Alexander T.</creatorcontrib><creatorcontrib>Dowley, Myles J. H.</creatorcontrib><creatorcontrib>Pradaux-Caggiano, Fabienne</creatorcontrib><creatorcontrib>Baldansuren, Amgalanbaatar</creatorcontrib><creatorcontrib>Fielding, Alistair J.</creatorcontrib><creatorcontrib>Tuna, Floriana</creatorcontrib><creatorcontrib>Hendon, Christopher H.</creatorcontrib><creatorcontrib>Walsh, Aron</creatorcontrib><creatorcontrib>Lloyd-Jones, Guy C.</creatorcontrib><creatorcontrib>John, Matthew P.</creatorcontrib><creatorcontrib>Carbery, David R.</creatorcontrib><collection>Istex</collection><collection>Wiley Online Library Open Access</collection><collection>CrossRef</collection><jtitle>Angewandte Chemie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murray, Alexander T.</au><au>Dowley, Myles J. H.</au><au>Pradaux-Caggiano, Fabienne</au><au>Baldansuren, Amgalanbaatar</au><au>Fielding, Alistair J.</au><au>Tuna, Floriana</au><au>Hendon, Christopher H.</au><au>Walsh, Aron</au><au>Lloyd-Jones, Guy C.</au><au>John, Matthew P.</au><au>Carbery, David R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B</atitle><jtitle>Angewandte Chemie</jtitle><addtitle>Angew. Chem</addtitle><date>2015-07-27</date><risdate>2015</risdate><volume>127</volume><issue>31</issue><spage>9125</spage><epage>9128</epage><pages>9125-9128</pages><issn>0044-8249</issn><eissn>1521-3757</eissn><abstract>The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan generates a catalyst system which facilitates biomimetic amine oxidation. Mechanistic and electron paramagnetic (EPR) spectroscopic data supports the conclusion that the reaction proceeds through a radical manifold. This data provides the first example of a biorelevant synthetic model for monoamine oxidase B activity.
MAO‐Nachahmer: Ein Modellflavin wird als Mimetikum der Monoaminoxidase B (MAO‐B) unter aeroben und Umgebungsbedingungen eingeführt. Kinetik‐ und EPR‐Studien geben Einblick in den Mechanismus: Ein geschwindigkeitsbestimmender Wasserstoffatomtransfer vom Amin zum Flavinakzeptor wird sowohl für das Modellsystem als auch für MAO‐B vorgeschlagen.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/ange.201503654</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0044-8249 |
| ispartof | Angewandte Chemie, 2015-07, Vol.127 (31), p.9125-9128 |
| issn | 0044-8249 1521-3757 |
| language | eng |
| recordid | cdi_crossref_primary_10_1002_ange_201503654 |
| source | Wiley-Blackwell Read & Publish Collection |
| subjects | Amine Enzyme EPR-Spektroskopie Oxidation Reaktionsmechanismen |
| title | Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T05%3A30%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-wiley_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Catalytic%20Amine%20Oxidation%20under%20Ambient%20Aerobic%20Conditions:%20Mimicry%20of%20Monoamine%20Oxidase%E2%80%85B&rft.jtitle=Angewandte%20Chemie&rft.au=Murray,%20Alexander%20T.&rft.date=2015-07-27&rft.volume=127&rft.issue=31&rft.spage=9125&rft.epage=9128&rft.pages=9125-9128&rft.issn=0044-8249&rft.eissn=1521-3757&rft_id=info:doi/10.1002/ange.201503654&rft_dat=%3Cwiley_cross%3EANGE201503654%3C/wiley_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c2784-830220b2528e27fafc861d4b0887296242616b5fa93bcd67658bf85e6bfcc85d3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |