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dc.contributor.author
Rivas, María G.
dc.contributor.author
González, Pablo J.
dc.contributor.author
Brondino, Carlos Dante
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dc.contributor.author
Moura, José J.G.
dc.contributor.author
Moura, Isabel
dc.date.available
2020-09-21T13:43:49Z
dc.date.issued
2007-12
dc.identifier.citation
Rivas, María G.; González, Pablo J.; Brondino, Carlos Dante; Moura, José J.G.; Moura, Isabel; EPR characterization of the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774 upon formate reduction; Elsevier Science Inc; Journal of Inorganic Biochemistry; 101; 11-12; 12-2007; 1617-1622
dc.identifier.issn
0162-0134
dc.identifier.uri
http://hdl.handle.net/11336/114394
dc.description.abstract
The EPR characterization of the molybdenum(V) forms obtained on formate reduction of both as-prepared and inhibited formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774, an enzyme that catalyzes the oxidation of formate to CO2, is reported. The Mo(V) EPR signal of the as-prepared formate-reduced enzyme is rhombic g max= 2.012, g mid=1.996, g min= 1.985 and shows hyperfine coupling with two nuclear species with I = 1/2. One of them gives an anisotropic splitting and is not solvent exchangeable (A max = 11.7, Amid= Amin = non detectable, A values in cm−1 x 10 −4). The second species is exchangeable with solvent and produces a splitting at the three principal g-values (Amax = 7.7, A mid = 10.0, A min = 9.3). The hyperfine couplings of the non-solvent and solvent exchangeable nuclei are assigned to the hydrogen atoms of the ƒÀ-methylene carbon of a selenocysteine and to a Mo ligand whose nature, sulfydryl or hydroxyl, is still in debate. The Mo(V) species obtained in the presence of inhibitors (azide or cyanide) yields a nearly axial EPR signal showing only one detectable splitting given by nuclear species with I= 1/2 (g max = 2.092, g mid = 2.000, g min = 1.989, A max = non-detectable, A mid = A min = 7.0), which is originated from the alpha-proton donated by the formate to a proximal ligand of the molybdenum. The possible structures of both paramagnetic molybdenum species (observed upon formate reduction in presence and absence of inhibitors) are discussed in comparison with the available structural information of this enzyme and the structural and EPR properties of the closely related formate dehydrogenase-H from Escherichia coli.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc
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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
DIMETHYLSULPHOXIDE REDUCTASE FAMILY
dc.subject
ELECTRON PARAMAGNETIC RESONANCE
dc.subject
FORMATE DEHYDROGENASE
dc.subject
MOLYBDENUM-CONTAINING ENZYMES
dc.subject.classification
Biofísica
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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
EPR characterization of the molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774 upon formate reduction
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-09-03T19:25:04Z
dc.journal.volume
101
dc.journal.number
11-12
dc.journal.pagination
1617-1622
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Rivas, María G.. Faculdade de Ciências E Tecnologia, Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: González, Pablo J.. Faculdade de Ciências E Tecnologia, Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Brondino, Carlos Dante. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Moura, José J.G.. Faculdade de Ciências E Tecnologia, Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Moura, Isabel. Faculdade de Ciências E Tecnologia, Universidade Nova de Lisboa; Portugal
dc.journal.title
Journal of Inorganic Biochemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGG-4NNWCC4-2&_user=2975255&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000057395&_version=1&_urlVersion=0&_userid=2975255&md5=df2eb74313beaab421f2ff3077693309
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jinorgbio.2007.04.011
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