EU TMR Programme funded network needs new post doctoral fellows or pre doctoral fellows until 30 Sept 2002
DIOXYGEN REACTIONS OF IRON-OXYGEN PROTEINS
IRON-OXYGEN PROTEIN NETWORK
Iron-oxygen clusters (m-oxo or m-hydroxo bridged di-iron clusters) are found in several iron-oxygen proteins. These biological iron-clusters are the sites for very difficult oxygenations of inert hydrocarbons at ambient temperature and pressure. Currently their potential use is limited due to stability problems and lack of knowledge of the reaction mechanism. The network will investigate the mechanism of industrially important oxygenation reactions carried out by the iron-oxygen proteins and small inorganic models with dioxygen and hydrogen peroxide. The network will mimic the reactions of the iron-oxygen cluster of the enzyme methane monooxygenase (MMO) from methanotrophic bacteria. The project aims at:
[1] to develop an understanding of the effects on the activity and function of modifications induced by rationally engineered MMO
[2] to determine the detailed reaction mechanism in MMO, by stabilizing reaction intermediates in the hydroxylation reaction with high resolution structural and spectroscopic studies
[3] to analyze and by rational design stabilize analogous intermediates in other iron-oxygen proteins or models,
[4] to develop a new approach to engineering of related but more stable iron-oxygen proteins, specially ribonucleotide reductase R2 protein (RNR-R2), into hydroxylation biocatalyst.
Training in a minimum two disciplines must be achieved by the young scientists (post docs/ students) in the network. The postdoctoral fellows will be required to present their work at the workshops and publications resulting from the joint efforts of the network. The goal is that the young scientists should be able to use a multi-disciplinary approach to solve complex problems. The network has 7 partners and 8 different groups. The TMR fellows must be a citizen of EU country or of Norway, Island, Liechtenstein or Israel. The TMR fellows must be working in a laboratory in a foreign country of which the person have not work for more than 18 months of the preceding the last 24 months. The person can not be 36 year of age or older when starting in the network. Please, contact the network participants directly by e-mail, fax or the coordinator (1, KKA) for further information. The most urgent positions are located in the following laboratories: Oslo (biophysics-enzymology), Warwick (microbiology), Stockholm (protein crystallography), Odense (industrial microbiology), Grenoble (model compounds), but less urgent positions are also available in biophysics and molecular biology (Stockholm, Lübeck).
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Partner name and affiliation |
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likely scientific speciality of the TMR fellow |
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1 ANDERSSON, K. Kristoffer,Univ. of Oslo, NO k.k.andersson@biokjemi.uio.no http://www.uio.no/~kkan/index.html Department of Biochemistry, University of Oslo, , PO Box 1041 Blindern, 0316 Oslo, Norway, Phone (+47)2285 6625, FAX (+47)2285 4443. The project will focus on the detailed oxygen activation reaction mechanisms and structural studies of particulate methane monooxygenase, and/or different ribonuclotide reductases methodology will be enzymology, magnetic and optical spectroscopy (EPR, ENDOR, Raman). |
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main: EPR, ENDOR, protein purification minor: Mössbauer spectroscopy, crystallography |
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2 DALTON, Howard,Univ. of Warwick, GB HD@dna.bio.warwick.ac.uk http://www.bio.warwick.ac.uk/dalton/ Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK, P (+44-2476) 523552, F (+44-2476) 523568. The project will focus on the detailed reaction mechanisms of methane monooxygenase, methodology will be microbiology, molecular biology, enzymology and studies of site directed mutants. |
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main: MMO, molecular biology minor: molecular biophysics |
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3 NORDLUND, Pär,Stockholm Univ., SE Par.Nordlund@dbb.su.se http://www.biokemi.su.se/research/Nordlund_Par.html Department of Biochemistry and biophysics, Stockholm University, Arrhenius laboratories, S-106 91 Stockholm, Sweden, P (+46-8) 164141, F (+46-8) 153679. The project will focus on solving 3D structures of the network protein, protein chemistry and crystallography of intermediates. |
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main: protein crystallography minor: enzymology, molecular biophysics |
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4 TRAUTWEIN, Alfred X.,Med. Univ. of Lübeck, DE trautwein@physik.mu-luebeck.de http://www.physik.mu-luebeck.de/ Institute of Physics, Medical University of Lübeck, Medizinische Universität, Institut für Physik, Ratzeburger Allee 160, D-23538 Lübeck, Germany, P (+49-451) 5004200, F (+49-451) 5004214. The project will focus on Mössbauer-, EPR-, magnetic susceptibility-, EXAFS-, and molecular orbital studies of iron clusters in biomolecules. |
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main: Mössbauer and EXAFS spectroscopy, theoretical calculations, minor: enzymology |
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5 JØRGENSEN, Lars,Norferm Denmark, DB-LAB, Odense, DK lars.jorgensen@norferm.com http://www.dblab.dk Norferm Denmark, Dansk Bioprotein A/S, Odense, Stenhuggervej 22, Postboks 829, DK-5230 Odense M, Denmark, P (+45) 65932920 , F (+45) 65932312. The project will focus on the methane monooxygenase and engineered biocatalysts in proteins and bacteria, methodology will be industrial microbiology, fermentation, molecular biology, large scale expression of biocatalysts and bioremediation. |
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main: industrial microbiology minor: molecular biology, enzymology |
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6 FONTECAVE, Marc,CEA and Univ. Joseph Fourier, Grenoble, FR fontecav@cbcrb.ceng.cea.fr http://www.ujf-grenoble.fr/ujf/fr/recherche/labujf/bscm.phtml CBCRB at CEA-Grenoble and Université Joseph Fourier, Grenoble Chimie et Biochimie des Centres Redox Biologiques, CBCRB, CEA-Grenoble, Bâtiment K, 17 Avenue des Martyrs F-38054 Grenoble Cedex 9, France, P (+33)- 4-7688 9103, F (+33) 4- 76889124. The project will focus on studies on small inorganic models containing iron clusters by Mössbauer-, EPR-, and other spectroscopic techniques. |
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main: small model complex chemistry minor: Mössbauer and EXAFS spectroscopy |
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7 GRÄSLUND, Astrid and SJÖBERG, Britt-Marie,Stockholm Univ., SE astrid.graslund@dbb.su.se http://www.biophys.su.se/ Department of Biochemistry and Biophysics, Stockholm University, Arrhenius laboratories, S-106 91 Stockholm, Sweden, P (+46-8) 162450, F (+46-8) 155597. The project will focus on ribonucleotide reductase by freeze quench and kinetical studies, oxygen activation, protein chemistry and spectroscopy (EPR, NMR). bitte@molbio.su.se http://www.molbio.su.se/ Department of Molecular Biology and Functional Genomics, Stockholm University, Arrhenius laboratories, S-106 91 Stockholm, Sweden, P (+46-8) 164150 , FAX (+46-8) 152350. The project will focus on mechanisms of coupled electron/proton transfer in proteins, the model system will be ribonucleotide reductase, and the methodology will be enzymology, gene technology and spectroscopy. |
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main and minor: molecular biophysics and/or molecular biology, RNR, Mössbauer and EXAFS spectroscopy, protein crystallography |
Short Summary of Scientific Network Highlights.
-A homologous and heterologous expression systems have been published 1999 for soluble methane monooxygenase and alkene monooxygenase, respectively. -First 3D structure, for the entire class of iron-oxygen proteins, of a diferrous azide (oxygen analogue) complex was published 1999 in J. Am. Chem. Soc., showing a carboxylate shift of the Fe2 ligand Glu 238 in the R2 protein in ribonucleotide reductase (RNR-R2). This allowed to refine the oxygen activating mechanism for this class of proteins. -Detection of a novel diferric cluster form by Mössbauer spectroscopy of E. coli F208Y RNR-R2. -Detection of a novel hydrogen bond network of the mouse RNR-R2 diferric cluster by resonance Raman published 1999 in J. Am. Chem. Soc., and by Mössbauer spectroscopy. -Detection of a novel diferric-peroxide complexed cluster in small inorganic model, analogous to the compound P in MMOH or RNR-R2 reactions with oxygen. - During the midterm review period (April 1998- April 2000) the network published over 50 publications with ISSN numbers directly related to the network (e.g. 7 in J. Biol. Chem.) + other related significant publications in top ranking journals, e.g. one in Science. See for instaceJoint network publications:Joint network publications.doc