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Biomimetic assembly and activation of [FeFe]-hydrogenases

Nature (London), 2013-07, Vol.499 (7456), p.66-69

2013

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A noble metal-free proton-exchange membrane fuel cell based on bio-inspired molecular catalysts

Chemical science (Cambridge), 2015-01, Vol.6 (3), p.2050-2053

2015

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Spectroscopic investigations of a semi-synthetic [FeFe] hydrogenase with propane di-selenol as bridging ligand in the binuclear subsite: comparison to the wild type and propane di-thiol variants

Journal of biological inorganic chemistry, 2018-05, Vol.23 (3), p.481-491

2018

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Is the presence of oxygen on an exoplanet a reliable biosignature?

Astrobiology, 2011-05, Vol.11 (4), p.335-341

2011

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Some general principles for designing electrocatalysts with hydrogenase activity

Coordination chemistry reviews, 2005-08, Vol.249 (15), p.1518-1535

2005

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Proton Electroreduction Catalyzed by Cobaloximes: Functional Models for Hydrogenases

Inorganic chemistry, 2005-06, Vol.44 (13), p.4786-4795

2005

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Immobilization of a Full Photosystem in the Large‐Pore MIL‐101 Metal–Organic Framework for CO2 reduction

ChemSusChem, 2018-09, Vol.11 (18), p.3315-3322

2018

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Superoxide Reductase from Desulfoarculus baarsii: Reaction Mechanism and Role of Glutamate 47 and Lysine 48 in Catalysis

Biochemistry (Easton), 2001-04, Vol.40 (16), p.5032-5040

2001

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Photocatalytic Carbon Dioxide Reduction with Rhodium-based Catalysts in Solution and Heterogenized within Metal-Organic Frameworks

ChemSusChem, 2015-02, Vol.8 (4), p.603-608

2015

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Pulse radiolysis studies on superoxide reductase from Treponema pallidum

FEBS letters, 2001-05, Vol.497 (2), p.171-173

2001

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Catalytic Transfer of Chiral Information from an Organic Compound to a Coordination Complex

ChemCatChem, 2010-12, Vol.2 (12), p.1533-1534

Fontecave, M.

2010

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[18] Ribonucleotide reductase from Pyrococcus furiosus

Methods in Enzymology, 2001, Vol.334, p.215-227

Fontecave, Marc

2001

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NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase

The Journal of biological chemistry, 1993-09, Vol.268 (25), p.18604-18609

1993

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Reaction of the NAD(P)H:Flavin Oxidoreductase from Escherichia coli with NADPH and Riboflavin: Identification of Intermediates

Biochemistry (Easton), 1998-08, Vol.37 (34), p.11879-11887

1998

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Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. Evidence for the catalytic role of serine 49 residue

The Journal of biological chemistry, 1996-07, Vol.271 (28), p.16656-61

1996

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Biotin Synthase Is a Pyridoxal Phosphate-Dependent Cysteine Desulfurase

Biochemistry (Easton), 2002-07, Vol.41 (29), p.9145-9152

2002

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Hydrolysis of Phosphodiesters by Diiron Complexes: Design of Nonequivalent Iron Sites in Purple Acid Phosphatase Models

Inorganic chemistry, 2003-01, Vol.42 (2), p.499-507

2003

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Sulfide Oxidation by Hydrogen Peroxide Catalyzed by Iron Complexes: Two Metal Centers Are Better Than One

Chemistry : a European journal, 2002-03, Vol.8 (5), p.1196-1204

2002

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Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module

Journal of molecular biology, 2000-05, Vol.299 (1), p.199-212

2000

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Caboloxime - Based photocatalytic Devices for Hydrogen Production

Angewandte Chemie International Edition, 2007, Vol.47 (3)

2007

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Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction

The Journal of biological chemistry, 1997-09, Vol.272 (39), p.24216-24223

1997

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Model complexes of di-iron sites in methane mono-oxygenase and ribonucleotide reductase: structure and reactivity

Biochemical Society transactions, 1997-02, Vol.25 (1), p.65-69

1997

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The Flavoprotein Component of the Escherichia coli Sulfite Reductase: Expression, Purification, and Spectral and Catalytic Properties of a Monomeric Form Containing both the Flavin Adenine Dinucleotide and the Flavin Mononucleotide Cofactors

Biochemistry (Easton), 1998-04, Vol.37 (17), p.6114-6123

1998

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Copper amine oxidase: a novel use for a tyrosine

Structure, 1995-11, Vol.3 (11), p.1127-1129

1995

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Reduction and mobilization of iron by a NAD(P)H: flavin oxidoreductase from Escherichia coli

European journal of biochemistry, 1993-02, Vol.211 (3), p.635-641

1993

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Biomimetic assembly and activation of [FeFe]-hydrogenases

A noble metal-free proton-exchange membrane fuel cell based on bio-inspired molecular catalysts

Spectroscopic investigations of a semi-synthetic [FeFe] hydrogenase with propane di-selenol as bridging ligand in the binuclear subsite: comparison to the wild type and propane di-thiol variants

Is the presence of oxygen on an exoplanet a reliable biosignature?

Some general principles for designing electrocatalysts with hydrogenase activity

Proton Electroreduction Catalyzed by Cobaloximes: Functional Models for Hydrogenases

Immobilization of a Full Photosystem in the Large‐Pore MIL‐101 Metal–Organic Framework for CO2 reduction

Superoxide Reductase from Desulfoarculus baarsii: Reaction Mechanism and Role of Glutamate 47 and Lysine 48 in Catalysis

Photocatalytic Carbon Dioxide Reduction with Rhodium-based Catalysts in Solution and Heterogenized within Metal-Organic Frameworks

Pulse radiolysis studies on superoxide reductase from Treponema pallidum

Catalytic Transfer of Chiral Information from an Organic Compound to a Coordination Complex

[18] Ribonucleotide reductase from Pyrococcus furiosus

NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase

Reaction of the NAD(P)H:Flavin Oxidoreductase from Escherichia coli with NADPH and Riboflavin: Identification of Intermediates

Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. Evidence for the catalytic role of serine 49 residue

Biotin Synthase Is a Pyridoxal Phosphate-Dependent Cysteine Desulfurase

Hydrolysis of Phosphodiesters by Diiron Complexes: Design of Nonequivalent Iron Sites in Purple Acid Phosphatase Models

Sulfide Oxidation by Hydrogen Peroxide Catalyzed by Iron Complexes: Two Metal Centers Are Better Than One

Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module

Caboloxime - Based photocatalytic Devices for Hydrogen Production

Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction

Model complexes of di-iron sites in methane mono-oxygenase and ribonucleotide reductase: structure and reactivity

The Flavoprotein Component of the Escherichia coli Sulfite Reductase: Expression, Purification, and Spectral and Catalytic Properties of a Monomeric Form Containing both the Flavin Adenine Dinucleotide and the Flavin Mononucleotide Cofactors

Copper amine oxidase: a novel use for a tyrosine

Reduction and mobilization of iron by a NAD(P)H: flavin oxidoreductase from Escherichia coli

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