Computational studies of enzymatic and biomimetic catalysts

Enzymes are the most efficient biocatalysts in Nature. However, biocatalysts in general are not capable of catalyzing reactions for industrial purposes. Hence, biocatalysts need to be engineered by introducing mutations in the active site or at distal positions in the enzyme, thereby inducing change...

Descripción completa

Detalles Bibliográficos
Autor: Romero Rivera, Adrian
Tipo de recurso: tesis doctoral
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:CBUC, CESCA
Repositorio:TDR. Tesis Doctorales en Red
OAI Identifier:oai:www.tdx.cat:10803/666175
Acceso en línea:http://hdl.handle.net/10803/666175
Access Level:acceso abierto
Palabra clave:Quàntums, Teoria dels
Mecánica cuántica
Quantum theory
Catalitzadors
Catalizadores
Catalysts
Enzims
Enzymes
Enzimas
Complexos biomimètics
Biomimetic complexes
Complejos biomiméticos
Espectroscòpia Mössbauer
Mössbauer spectroscopy
Espectroscopia Mössbauer
544
id ES_2b2bf55fb4274e866fa60dcfcffc2d44
oai_identifier_str oai:www.tdx.cat:10803/666175
network_acronym_str ES
network_name_str España
repository_id_str
spelling Computational studies of enzymatic and biomimetic catalystsRomero Rivera, AdrianQuàntums, Teoria delsMecánica cuánticaQuantum theoryCatalitzadorsCatalizadoresCatalystsEnzimsEnzymesEnzimasComplexos biomimèticsBiomimetic complexesComplejos biomiméticosEspectroscòpia MössbauerMössbauer spectroscopyEspectroscopia Mössbauer544Enzymes are the most efficient biocatalysts in Nature. However, biocatalysts in general are not capable of catalyzing reactions for industrial purposes. Hence, biocatalysts need to be engineered by introducing mutations in the active site or at distal positions in the enzyme, thereby inducing changes in the conformational dynamics of enzymes. In this thesis an analysis of conformational dynamics of several enzymes has been developed by using computational tools for understanding how their conformational dynamics affect the enzyme function. Biomimetic chemistry seeks to design novel efficient metal-based organocatalysts mimicking the structure-function from the enzyme’s active site. In this thesis detailed mechanism pathways for EUK-8 salen ligand have been proposed through computational tools. 57Fe Mössbauer spectroscopy is a technique that provides information about the chemical nature of Iron systems, regardless of its spin and oxidation states. Since the Mössbauer spectra is not always straightforward to analyze, this new computational analysis performed will support experimental Mössbauer data for helping to characterize Fe-based systems.Els enzims són els catalitzadors més eficients que existeixen a la Natura. No obstant, en general no són capaços de catalitzar reaccions importants per a propòsits industrials. Per tant, calen ser modificats introduint mutacions en el centre actiu o en posicions llunyanes, alterant així la seva dinàmica conformacional. En aquesta tesi s'ha realitzat un anàlisi centrat en la dinàmica conformacional de diferents enzims fent servir eines computacionals. La química biomimètica cerca dissenyar nous organocatalitzadors eficients imitant la funció estructural del centre actiu de l’enzim. En aquesta tesi es presenta el mecanisme detallat pel lligand EUK-8 salen per tal de poder-ne millorar la seva activitat catalasa. L’espectroscòpia Mössbauer de 57Fe és una tècnica que proporciona informació sobre la naturalesa química dels sistemes de Ferro, respecte els estat d’espín i d’oxidació. Com que els espectres de Mössbauer no sempre són fàcils d’analitzar, el nou mètode desenvolupat ajudarà a analitzar les dades experimentals de Mössbauer i també a caracteritzar les diferents espècies de Fe.Universitat de GironaSwart, MarcelOsuna Oliveras, SílviaSwart, MarcelUniversitat de Girona. Institut de Química Computacional i Catàlisi201920192018info:eu-repo/semantics/doctoralThesisinfo:eu-repo/semantics/publishedVersion189 p.application/pdfapplication/pdfhttp://hdl.handle.net/10803/666175TDX (Tesis Doctorals en Xarxa)reponame:TDR. Tesis Doctorales en Redinstname:CBUC, CESCAInglésL'accés als continguts d'aquesta tesi queda condicionat a l'acceptació de les condicions d'ús establertes per la següent llicència Creative Commons: http://creativecommons.org/licenses/by-nc/4.0/http://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:www.tdx.cat:10803/6661752026-06-14T12:46:07Z
dc.title.none.fl_str_mv Computational studies of enzymatic and biomimetic catalysts
title Computational studies of enzymatic and biomimetic catalysts
spellingShingle Computational studies of enzymatic and biomimetic catalysts
Romero Rivera, Adrian
Quàntums, Teoria dels
Mecánica cuántica
Quantum theory
Catalitzadors
Catalizadores
Catalysts
Enzims
Enzymes
Enzimas
Complexos biomimètics
Biomimetic complexes
Complejos biomiméticos
Espectroscòpia Mössbauer
Mössbauer spectroscopy
Espectroscopia Mössbauer
544
title_short Computational studies of enzymatic and biomimetic catalysts
title_full Computational studies of enzymatic and biomimetic catalysts
title_fullStr Computational studies of enzymatic and biomimetic catalysts
title_full_unstemmed Computational studies of enzymatic and biomimetic catalysts
title_sort Computational studies of enzymatic and biomimetic catalysts
dc.creator.none.fl_str_mv Romero Rivera, Adrian
author Romero Rivera, Adrian
author_facet Romero Rivera, Adrian
author_role author
dc.contributor.none.fl_str_mv Swart, Marcel
Osuna Oliveras, Sílvia
Swart, Marcel
Universitat de Girona. Institut de Química Computacional i Catàlisi
dc.subject.none.fl_str_mv Quàntums, Teoria dels
Mecánica cuántica
Quantum theory
Catalitzadors
Catalizadores
Catalysts
Enzims
Enzymes
Enzimas
Complexos biomimètics
Biomimetic complexes
Complejos biomiméticos
Espectroscòpia Mössbauer
Mössbauer spectroscopy
Espectroscopia Mössbauer
544
topic Quàntums, Teoria dels
Mecánica cuántica
Quantum theory
Catalitzadors
Catalizadores
Catalysts
Enzims
Enzymes
Enzimas
Complexos biomimètics
Biomimetic complexes
Complejos biomiméticos
Espectroscòpia Mössbauer
Mössbauer spectroscopy
Espectroscopia Mössbauer
544
description Enzymes are the most efficient biocatalysts in Nature. However, biocatalysts in general are not capable of catalyzing reactions for industrial purposes. Hence, biocatalysts need to be engineered by introducing mutations in the active site or at distal positions in the enzyme, thereby inducing changes in the conformational dynamics of enzymes. In this thesis an analysis of conformational dynamics of several enzymes has been developed by using computational tools for understanding how their conformational dynamics affect the enzyme function. Biomimetic chemistry seeks to design novel efficient metal-based organocatalysts mimicking the structure-function from the enzyme’s active site. In this thesis detailed mechanism pathways for EUK-8 salen ligand have been proposed through computational tools. 57Fe Mössbauer spectroscopy is a technique that provides information about the chemical nature of Iron systems, regardless of its spin and oxidation states. Since the Mössbauer spectra is not always straightforward to analyze, this new computational analysis performed will support experimental Mössbauer data for helping to characterize Fe-based systems.
publishDate 2018
dc.date.none.fl_str_mv 2018
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/doctoralThesis
info:eu-repo/semantics/publishedVersion
format doctoralThesis
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10803/666175
url http://hdl.handle.net/10803/666175
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by-nc/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 189 p.
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Universitat de Girona
publisher.none.fl_str_mv Universitat de Girona
dc.source.none.fl_str_mv TDX (Tesis Doctorals en Xarxa)
reponame:TDR. Tesis Doctorales en Red
instname:CBUC, CESCA
instname_str CBUC, CESCA
reponame_str TDR. Tesis Doctorales en Red
collection TDR. Tesis Doctorales en Red
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869405127583989760
score 15.300719