Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme
We report the full reduction of the biological cofactor FMN with visible light using CdSe quantum dots and methylviologen as an electron relay. In turn, these reducing equivalents can drive the stereospecific reduction of ketoisophorone by an old yellow enzyme homologue from Bacillus subtilis (YqjM)...
- Autores:
-
Panay Escobar, Aram Joel
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2012
- Institución:
- Universidad ICESI
- Repositorio:
- Repositorio ICESI
- Idioma:
- eng
- OAI Identifier:
- oai:repository.icesi.edu.co:10906/79886
- Acceso en línea:
- http://pubs.acs.org/doi/abs/10.1021/cs300085h
http://hdl.handle.net/10906/79886
https://doi.org/10.1021/cs300085h
- Palabra clave:
- Enzimas
Bacillus
Bacillus subtillis
Cetoisoforona
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by-nc-nd/4.0/
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Panay Escobar, Aram JoelNueva York, de Lat: 30 37 00 N degrees minutes Lat: 30.6167 decimal degrees Long: 115 51 00 W degrees minutes Long: -115.8500 decimal degrees2016-08-30T22:01:56Z2016-08-30T22:01:56Z2012-03-192910–2919http://pubs.acs.org/doi/abs/10.1021/cs300085hhttp://hdl.handle.net/10906/79886https://doi.org/10.1021/cs300085hinstname: Universidad Icesireponame: Biblioteca Digitalrepourl: https://repository.icesi.edu.co/We report the full reduction of the biological cofactor FMN with visible light using CdSe quantum dots and methylviologen as an electron relay. In turn, these reducing equivalents can drive the stereospecific reduction of ketoisophorone by an old yellow enzyme homologue from Bacillus subtilis (YqjM). The experiments demonstrate the current capabilities and limitations of quantum dots as part of a cofactor regeneration system and pave the road for future studies aimed at new and improved in situ light-driven cofactor regeneration strategies.3 páginasDigitalapplication/pdfengAmerican Chemical SocietyFacultad de Ciencias NaturalesBiologíaDepartamento de Ciencias BiológicasNueva YorkAcs Catalysis, Vol. 2, No. 4 - 2012EL AUTOR, expresa que la obra objeto de la presente autorización es original y la elaboró sin quebrantar ni suplantar los derechos de autor de terceros, y de tal forma, la obra es de su exclusiva autoría y tiene la titularidad sobre éste. PARÁGRAFO: en caso de queja o acción por parte de un tercero referente a los derechos de autor sobre el artículo, folleto o libro en cuestión, EL AUTOR, asumirá la responsabilidad total, y saldrá en defensa de los derechos aquí autorizados; para todos los efectos, la Universidad Icesi actúa como un tercero de buena fe. Esta autorización, permite a la Universidad Icesi, de forma indefinida, para que en los términos establecidos en la Ley 23 de 1982, la Ley 44 de 1993, leyes y jurisprudencia vigente al respecto, haga publicación de este con fines educativos. Toda persona que consulte ya sea la biblioteca o en medio electrónico podrá copiar apartes del texto citando siempre la fuentes, es decir el título del trabajo y el autor.https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessAtribución-NoComercial-SinDerivadas 4.0 Internacional (CC BY-NC-ND 4.0)http://purl.org/coar/access_right/c_abf2EnzimasBacillusBacillus subtillisCetoisoforonaLight-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzymeinfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1Artículoinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/version/c_970fb48d4fbd8a85Comunidad Universidad Icesi – Investigadores26673ORIGINALdocumento.htmldocumento.htmltext/html296http://repository.icesi.edu.co/biblioteca_digital/bitstream/10906/79886/1/documento.htmlbbd613f943c8de1778c25addbde955c5MD5110906/79886oai:repository.icesi.edu.co:10906/798862018-11-26 14:45:48.203Biblioteca Digital - Universidad icesicdcriollo@icesi.edu.co |
| dc.title.spa.fl_str_mv |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| title |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| spellingShingle |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme Enzimas Bacillus Bacillus subtillis Cetoisoforona |
| title_short |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| title_full |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| title_fullStr |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| title_full_unstemmed |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| title_sort |
Light-Driven, Quantum Dot-Mediated Regeneration of FMN To Drive Reduction of Ketoisophorone by Old Yellow Enzyme |
| dc.creator.fl_str_mv |
Panay Escobar, Aram Joel |
| dc.contributor.author.spa.fl_str_mv |
Panay Escobar, Aram Joel |
| dc.subject.none.fl_str_mv |
Enzimas Bacillus Bacillus subtillis Cetoisoforona |
| topic |
Enzimas Bacillus Bacillus subtillis Cetoisoforona |
| description |
We report the full reduction of the biological cofactor FMN with visible light using CdSe quantum dots and methylviologen as an electron relay. In turn, these reducing equivalents can drive the stereospecific reduction of ketoisophorone by an old yellow enzyme homologue from Bacillus subtilis (YqjM). The experiments demonstrate the current capabilities and limitations of quantum dots as part of a cofactor regeneration system and pave the road for future studies aimed at new and improved in situ light-driven cofactor regeneration strategies. |
| publishDate |
2012 |
| dc.date.issued.none.fl_str_mv |
2012-03-19 |
| dc.date.accessioned.none.fl_str_mv |
2016-08-30T22:01:56Z |
| dc.date.available.none.fl_str_mv |
2016-08-30T22:01:56Z |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article |
| dc.type.coar.none.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
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Artículo |
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info:eu-repo/semantics/publishedVersion |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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publishedVersion |
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2910–2919 |
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http://pubs.acs.org/doi/abs/10.1021/cs300085h |
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http://hdl.handle.net/10906/79886 |
| dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1021/cs300085h |
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instname: Universidad Icesi |
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reponame: Biblioteca Digital |
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repourl: https://repository.icesi.edu.co/ |
| identifier_str_mv |
2910–2919 instname: Universidad Icesi reponame: Biblioteca Digital repourl: https://repository.icesi.edu.co/ |
| url |
http://pubs.acs.org/doi/abs/10.1021/cs300085h http://hdl.handle.net/10906/79886 https://doi.org/10.1021/cs300085h |
| dc.language.iso.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.ispartof.none.fl_str_mv |
Acs Catalysis, Vol. 2, No. 4 - 2012 |
| dc.rights.uri.none.fl_str_mv |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
| dc.rights.accessrights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| dc.rights.license.none.fl_str_mv |
Atribución-NoComercial-SinDerivadas 4.0 Internacional (CC BY-NC-ND 4.0) |
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http://purl.org/coar/access_right/c_abf2 |
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https://creativecommons.org/licenses/by-nc-nd/4.0/ Atribución-NoComercial-SinDerivadas 4.0 Internacional (CC BY-NC-ND 4.0) http://purl.org/coar/access_right/c_abf2 |
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openAccess |
| dc.format.extent.none.fl_str_mv |
3 páginas |
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Digital |
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application/pdf |
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Nueva York, de Lat: 30 37 00 N degrees minutes Lat: 30.6167 decimal degrees Long: 115 51 00 W degrees minutes Long: -115.8500 decimal degrees |
| dc.publisher.spa.fl_str_mv |
American Chemical Society |
| dc.publisher.faculty.none.fl_str_mv |
Facultad de Ciencias Naturales |
| dc.publisher.program.none.fl_str_mv |
Biología |
| dc.publisher.department.none.fl_str_mv |
Departamento de Ciencias Biológicas |
| dc.publisher.place.none.fl_str_mv |
Nueva York |
| institution |
Universidad ICESI |
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http://repository.icesi.edu.co/biblioteca_digital/bitstream/10906/79886/1/documento.html |
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