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Institutes/ Institute of life sciences research and technologies (iRTSV)/ Unités / Chimie et Biologie des Métaux (CBM)/ Physicochemistry of metals in biology

Physicochemistry of metals in biology



Group leader
 

Dr. Jean-Marc Latour
CEA Researcher

iRTSV/LCBM
CEA Grenoble
17 rue des Martyrs
38 054 Grenoble Cedex
Phone: 04 38 78 44 07
email: Jean-Marc.Latour@cea.fr

Secretary
Phone: (33) 4 38 78 21 44
Fax: (33) 4 38 78 54 65
 
About a third of proteins are known to harbor at their active site a metal that is essential for their fonction and confer them characteristic physical properties which reflect how the protein surrounds it and how its environment is modified. As a consequence a thorough study of these properties is of utmost interest since it provides essential clues to understand both the structure and the function of the metalloprotein. To translate these physical properties into structural and functional parameters, it is necessary to establish sound correlations from the study of perfectly characterized synthetic models. It results that this field is deeply interdisciplinary, mixing both the concepts and the methods of biology, chemistry and molecular physics.

Our team associates expertises in molecular and structural biology, organic, inorganic and physical chemistry and in magnetic resonance spectroscopies to contribute to improving how metalloproteins and model complexes operate in dealing with hydrogen peroxide and related reagents. Its research activities encompass:

  • the structural and functional study of the bacterial peroxide sensor PerR
  • reactivity studies of protein cysteinate zinc sites through the use of model peptides
  • reactivity studies of biomimetic diiron complexes enganged in catalytic imide transfers and their extension as amine sensors
  • spectroscopic and magnetic studies of manganese and iron proteins and model complexes.

The latter activity relies heavily on the use of our Mössbauer platform dedicated to the characterization of iron proteins and implies numerous national and international collaborations.

 
Transition metal ions exhibit unique redox and spectroscopic properties owing to the fact that they possess partially filled d orbital shells. Indeed, electrons in these high energy levels can be exchanged easily and this feature explains why iron, manganese and copper are present in numerous proteins involved in electron transfers and redox activities. Conversely, open d shells allow electronic transitions both within the metal d levels and from (or to) the ligands, which give rise, respectively, to d-d transitions and Ligand-to-Metal Charge Transfer (or Metal-to-Ligand Charge Transfer) transitions. In addition, numerous electronic configurations of these metal species involve an odd number of electrons. As a consequence, they possess characteristic magnetic properties which can be studied by magnetic spectroscopies.
 
Group members
 
 
PhD thesis
 

2011
Michaël Carboni.
A biomimetic approach to study Iron-Manganese enzymes.
[Abstract] [Thesis on line]

2008
Éric Gouré.
Amine transfer reactions catalyzed by binuclear non heme iron systems: High oxidation state intermediates.
[Abstract] [Thesis on line]

Daouda Traore.
Structural studies of the PerR protein: A metalloprotein sensor of H2O2.
[Abstract] [Thesis on line]

2007
Abdelnasser El Ghazouani.
Biochemical and functional characterizations of the PerR protein (Bacillus subtilis): A bacterial sensor of hydrogen peroxide.
[Abstract] [Thesis on line]

2005
Nadia Abed.
The Fur protein, a new antibacterial target ? Approach using petide aptamers..
[Abstract]

2003
Frédéric Avenier.
Étude mécanistique des réactions de transfert d'oxygène et d'amine catalysées par des complexes dinucléaires de fer : biomimétisme et catalyse.
[Abstract]

2002
Benoît d’Autréaux.
Spectroscopic studies of the Fur protein (Ferric Uptake regulation). Interaction with nitric oxide.
[Abstract]

2001
Lionel Dubois.
Synthèse et étude de complexes biomimétiques du site actif des catalases à manganèse : étude mécanistique de la réaction de dismutation du peroxyde d'hydrogène.
[Abstract]

2000
Anne Gonzalez de Peredo.
Étude structurale de al protéine FUR (Ferric Uptake Regulation) d’Escherichia coli par spectrométrie de masse.
 
Key words
 
Metalloproteins, chemical models, oxidative stress, peptides, EPR, Mössbauer, spectroscopy
 
Publications