Responsable: Ernesto Carmona Guzmán
Tipo de Proyecto/Ayuda: 6º Programa Marco de la U.E.
Referencia: MOIF-CT-2004-509334
Web: http://cordis.europa.eu/projects/rcn/73533_en.html
Fecha de Inicio: 01-06-2004
Fecha de Finalización: 31-05-2007

Empresa/Organismo financiador/es:

• Commission of the European Communities (Marie Curie International Fellowships)

Socios:

• Stanford University (Edward I. Solomon)

Contratados:

• Investigadores:
  • Diego del Río Díaz-Jara

Resumen del proyecto:

Copper sites in Biology are involved in a wide variety of functions including reversible O2 binding,activation for hydroxylation and cofactor formation, the four electron reduction of O2 to H2O and two electronreduction of N2O to N2. Copper proteins often exhibit unique spectroscopie features which reflect novelgeometric and electronic structures (i.e. highly covalent bonds and exchange couplings between metal centers inclusters) which make major contributions to function. This research projects emphasised on the combination ofabsorption, variable-temperature variable-field magnetic circular dichroism (MCD), resonance Raman (rR),electron paramagnetic resonance (EPR), SQUID magnetic susceptibility, X-ray absorption (XAS), and relatedspectroscopies in parallel with density functional theory (DFT) calculations to define these active sites in theproteins and relevant model complexes and their intermediates to determine geometric and electronic structurecontributions to reactivity. These studies will define structure/function correlations, provide molecular levelinsight into metal metabolism, disease states and possible drug inhibitors and provide the basis for newhomogeneous and biotech catalysts.The specific aims for this research project are:1) Extend our spectroscopie and computational studies on Cu(II)-OOR model complexes to the non-coupled binuclear Cu enzymes dopamine ?-monooxygenase and peptidylglycine a-hydroxylatingmonooxygenase to understand how O2 is activated for hydroxylation by a single Cu center.2) Define O2 intermediates in heme/Cu model complexes and their perturbation by ligand variation toobtain molecular level insight into O2 reduction to water by cytochrome c oxidase in parallel to ourstudies on the reaction coordinate of the multicopper oxidases.