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dc.contributor.author
Marangon, Jacopo
dc.contributor.author
Correia, Hugo D.
dc.contributor.author
Brondino, Carlos Dante
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dc.contributor.author
Moura, José J. G.
dc.contributor.author
Romão, Maria J.
dc.contributor.author
González, Pablo Javier
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dc.contributor.author
Santos Silva, Teresa
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dc.date.available
2015-05-19T13:17:15Z
dc.date.issued
2013-12-31
dc.identifier.citation
Marangon, Jacopo; Correia, Hugo D.; Brondino, Carlos Dante; Moura, José J. G.; Romão, Maria J.; et al.; Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H2O2; Public Library of Science; Plos One; 8; 12; 31-12-2013; 1-11; e83234
dc.identifier.issn
1932-6203
dc.identifier.uri
http://hdl.handle.net/11336/494
dc.description.abstract
Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and heterocyclic compounds. The molybdenum active site shows a distorted square-pyramidal geometry in which two ligands, a hydroxyl/water molecule (the catalytic labile site) and a sulfido ligand, have been shown to be essential for catalysis. The XO family member aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is an exception as presents in its catalytically competent form an equatorial oxo ligand instead of the sulfido ligand. Despite this structural difference, inactive samples of DgAOR can be activated upon incubation with dithionite plus sulfide, a procedure similar to that used for activation of desulfo-XO. The fact that DgAOR does not need a sulfido ligand for catalysis indicates that the process leading to the activation of inactive DgAOR samples is different to that of desulfo-XO. We now report a combined kinetic and X-ray crystallographic study to unveil the enzyme modification responsible for the inactivation and the chemistry that occurs at the Mo site when Dg AOR is activated. In contrast to XO, which is activated by resulfuration of the Mo site, DgAOR activation/inactivation is governed by the oxidation state of the dithiolene moiety of the pyranopterin cofactor, which demonstrates the non-innocent behavior of the pyranopterin in enzyme activity. We also showed that Dg AOR incubation with dithionite plus sulfide in the presence of dioxygen produces hydrogen peroxide not associated with the enzyme activation. The peroxide molecule coordinates to molybdenum in a η2 fashion inhibiting the enzyme activity.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library of Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Molybdenum
dc.subject
Molybdenum-Enzymes
dc.subject
Aldehyde Oxidoreductase
dc.subject
Xanthine Oxidase
dc.subject
Enzyme Kinetics
dc.subject
X-Ray Crystallography
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H2O2
dc.type
info:eu-repo/semantics/publishedVersion
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dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/article
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dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
8
dc.journal.number
12
dc.journal.pagination
1-11; e83234
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
San Francisco
dc.description.fil
Fil: Marangon, Jacopo. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Correia, Hugo D.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Moura, José J. G.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Romão, Maria J.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: González, Pablo Javier. Universidade Nova de Lisboa; Portugal. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Santos Silva, Teresa. Universidade Nova de Lisboa; Portugal
dc.journal.title
Plos One
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pone.0083234
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0083234
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