Pablo J. González

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Desulfovibrio gigas aldehyde oxidoreductase (DgAOR) is a mononuclear molybdenum-containing enzyme from the xanthine oxidase (XO) family, a group of enzymes capable of catalyzing the oxidative hydroxylation of aldehydes and heterocyclic compounds. The kinetic studies reported in this work showed that DgAOR catalyzes the oxidative hydroxylation of aromatic(More)
Volcano observatories provide near real-time information and, ultimately, forecasts about volcano activity. For this reason, multiple physical and chemical parameters are continuously monitored. Here, we present a new method to efficiently estimate the location and evolution of magmatic sources based on a stream of real-time surface deformation data, such(More)
The authors would like to publish an erratum to include the additional text in the acknowledgement section. members of CONICET (Argentina). We thank the beam-line scientists of ID29 from the ESRF and of Proxima I from SOLEIL for their assistance in X-ray data collection.
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(More)
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(More)
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