ACTIVOXY

Oxygen Activation in Ribonucleotide Reductase and Multicopper Oxidases Proteins

Coordinatore	UNIVERSITETET I OSLO    more  Organization address address: Problemveien 5-7 city: OSLO postcode: 313 contact info Titolo: Ms. Nome: Kate Cognome: Bronndal Email: send email Telefono: -22854626 Fax: -22855994
Nazionalità Coordinatore	Norway [NO]
Totale costo	0 €
EC contributo	202˙542 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-IEF-2008
Funding Scheme	MC-IEF
Anno di inizio	2009
Periodo (anno-mese-giorno)	2009-06-01   -   2011-05-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	UNIVERSITETET I OSLO  Organization address address: Problemveien 5-7 city: OSLO postcode: 313 contact info Titolo: Ms. Nome: Kate Cognome: Bronndal Email: send email Telefono: -22854626 Fax: -22855994	NO (OSLO)	coordinator	202˙542.89

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 Obiettivo del progetto (Objective)

'Boundaries among biological, chemical and physical domains are nowadays fading, and the complex phenomena observed in Nature as well as in artificial systems can only be tackled from a broader/interdisciplinary perspective. In this context, the biological activation of the molecular oxygen is a fascinating and yet complex process. The ability to store, transport and utilize this simple molecule gated evolution of life in our planet and led to growth and selection of a variety of organisms. Complex molecules selected by Nature as active in “key metabolic paths” of the oxygen in life often contain copper and/or iron metal ions as reactive centres. A wide variety of experimental results and theoretical investigations show that the metallo-oxygen interactions have dominant states that are not spatially homogeneous (anisotropy). These effects occur when a number of physical interactions such as spin, charge, lattice (crystal-field), and/or orbitals are simultaneously active. The result of these interlocked numbers of factors links biology to chemistry and molecular physic, and allow the oxygen to be used in different ways within metabolism. The research proposal presented herein aims to investigate the red/ox mechanism and the connected energetic of the oxygen activation process in a series of di-iron (Ribonucleotide Reductase, RNR, Class I R2) and copper protein (multicopper oxidases) through the use of spectroscopic methods (EPR X-Q, high field EPR, CD, MCD, rR resonance Raman), structural (X-ray) and kinetic analyses (stopped flow, cryoenzymology). The endeavour is directed towards a better understanding of the geometric and electronic structure of metal-oxygen interactions that contribute to define O2 reactivity. These studies will provide molecular level insight into oxygen and metal metabolism, disease states, bioremediation and possible the development of efficient drugs inhibitor.'