caa a22 4500 605507821 CHVBK 20210128100633.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1204-8 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1204-8 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 [Elektronische Daten] [María Gómez, Nicolás Neuman, Sergio Dalosto, Pablo González, José Moura, Alberto Rizzi, Carlos Brondino] 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. SBIC, 2014 Aldehyde oxidoreductase nationallicence Molybdenum nationallicence Exchange interaction nationallicence EPR nationallicence QM/MM nationallicence Dg AOR : Aldehyde oxidoreductase from Desulfovibrio gigas nationallicence Gómez María Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut Neuman Nicolás Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut Dalosto Sergio Instituto de Física del Litoral, CONICET-UNL, Güemes 3450, S3000ZAA, Santa Fe, Argentina aut González Pablo Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut Moura José REQUIMTE/CQFB, Departamento de Quimica, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut Rizzi Alberto Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut Brondino Carlos Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 233-242 0949-8257 20:2<233 2015 20 775 https://doi.org/10.1007/s00775-014-1204-8 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1204-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gómez María Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- Neuman Nicolás Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- Dalosto Sergio Instituto de Física del Litoral, CONICET-UNL, Güemes 3450, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- González Pablo Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- Moura José REQUIMTE/CQFB, Departamento de Quimica, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 700 1- Rizzi Alberto Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 700 1- Brondino Carlos Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Ciudad Universitaria, Paraje El Pozo, S3000ZAA, Santa Fe, Argentina aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 233-242 0949-8257 20:2<233 2015 20 775