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dc.contributor.author
Gomez, María C.
dc.contributor.author
Neuman, Nicolás Ignacio
dc.contributor.author
Dalosto, Sergio Daniel
dc.contributor.author
González, Pablo Javier
dc.contributor.author
Moura, Jose J. G.
dc.contributor.author
Rizzi, Alberto C.
dc.contributor.author
Brondino, Carlos
dc.date.available
2017-02-03T21:14:06Z
dc.date.issued
2014-10
dc.identifier.citation
Gomez, María C.; Neuman, Nicolás Ignacio; Dalosto, Sergio Daniel; González, Pablo Javier; Moura, Jose J. G.; et al.; Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study; Springer; Journal Of Biological Inorganic Chemistry; 20; 2; 10-2014; 233-242
dc.identifier.issn
0949-8257
dc.identifier.uri
http://hdl.handle.net/11336/12512
dc.description.abstract
Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and FeS 2. The electron transfer reaction inside DgAOR is proposed to be performed through a chemical pathway linking Mo and the two FeS clusters involving the pyranopterin ligand. EPR studies performed on reduced as-prepared DgAOR showed that this pathway is able to transmit very weak exchange interactions between Mo(V) and reduced FeS 1. Similar EPR studies but performed on DgAOR samples inhibited with glycerol and ethylene glycol showed that the value of the exchange coupling constant J increases ~2 times upon alcohol inhibition. Structural studies in these DgAOR samples have demonstrated that the Mo–FeS 1 bridging pathway does not show significant differences, confirming that the changes in J observed upon inhibition cannot be ascribed to structural changes associated neither with pyranopterin and FeS 1 nor with changes in the electronic structure of FeS 1, as its EPR properties remain unchanged. Theoretical calculations indicate that the changes in J detected by EPR are related to changes in the electronic structure of Mo(V) determined by the replacement of the OHx labile ligand for an alcohol molecule. Since the relationship between electron transfer rate and isotropic exchange interaction, the present results suggest that the intraenzyme electron transfer process mediated by the pyranopterin moiety is governed by a Mo ligand-based regulatory mechanism.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Aldehyde Oxidoreductase
dc.subject
Molybdenum
dc.subject
Exchange Interaction
dc.subject
Epr
dc.subject
Qm/Mm
dc.subject.classification
Biofísica
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-02-23T16:44:35Z
dc.journal.volume
20
dc.journal.number
2
dc.journal.pagination
233-242
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Gomez, María C.. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
dc.description.fil
Fil: Neuman, Nicolás Ignacio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Dalosto, Sergio Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Física del Litoral; Argentina
dc.description.fil
Fil: González, Pablo Javier. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Moura, Jose J. G.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Rizzi, Alberto C.. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
dc.description.fil
Fil: Brondino, Carlos. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
dc.journal.title
Journal Of Biological Inorganic Chemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s00775-014-1204-8
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1007/s00775-014-1204-8


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