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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Winfried LEIBL : Photocatalyse et Biohydrogène

Publications de l’équipe

2017


  • R. Martin, F. Lacombat, A. Espagne, N. Dozova, P. Plaza, J. Yamamoto, P. Müller, K. Brettel, et A. de la Lande, « Ultrafast flavin photoreduction in an oxidized animal (6-4) photolyase through an unconventional tryptophan tetrad », Physical chemistry chemical physics: PCCP, 2017.
    Résumé : Photolyases are flavoenzymes repairing UV-induced lesions in DNA, which may be activated by a photoreduction of their FAD cofactor. In most photolyases, this photoreduction proceeds by electron transfer along a chain of three tryptophan (Trp) residues, connecting the flavin to the protein surface. Much less studied, animal (6-4) photolyases (repairing pyrimidine-pyrimidone (6-4) photoproducts) are particularly interesting as they were recently shown to have a longer electron transfer chain, counting four Trp residues. Using femtosecond polarized transient absorption spectroscopy, we performed a detailed analysis of the photoactivation reaction in the (6-4) photolyase of Xenopus laevis with oxidized FAD. We showed that the excited flavin is very quickly reduced (∼0.5 ps) by a nearby tryptophan residue, yielding FAD˙(-) and WH˙(+) radicals. Subsequent kinetic steps in the picosecond regime were assigned to the migration of the positive charge along the Trp tetrad, in competition with charge recombination. We propose that the positive charge is actually delocalized over various Trp residues during most of the dynamics and that charge recombination essentially occurs through the proximal tryptophanyl radical. Oxidation of the fourth tryptophan is thought to be reached about as fast as that of the third one (∼40 ps), based on a comparison with a mutant protein lacking the distal Trp, implying ultrafast electron transfer between these two residues. This unusual mechanism sheds light on the rich diversity of electron transfer pathways found in various photolyases, and evolution-related cryptochromes alike.
    Mots-clés : B3S, LPB.

  • A. Mezzetti et W. Leibl, « Time-resolved infrared spectroscopy in the study of photosynthetic systems », Photosynthesis Research, vol. 131, nᵒ 2, p. 121-144, 2017.
    Résumé : Time-resolved (TR) infrared (IR) spectroscopy in the nanosecond to second timescale has been extensively used, in the last 30 years, in the study of photosynthetic systems. Interesting results have also been obtained at lower time resolution (minutes or even hours). In this review, we first describe the used techniques-dispersive IR, laser diode IR, rapid-scan Fourier transform (FT)IR, step-scan FTIR-underlying the advantages and disadvantages of each of them. Then, the main TR-IR results obtained so far in the investigation of photosynthetic reactions (in reaction centers, in light-harvesting systems, but also in entire membranes or even in living organisms) are presented. Finally, after the general conclusions, the perspectives in the field of TR-IR applied to photosynthesis are described.
    Mots-clés : B3S, Bacterial reaction centers, Carotenoids, Chlorophyll, Electron transfer, FTIR difference spectroscopy, Infrared, Kinetics, Light-harvesting systems, LPB, photosynthesis, Photosynthetic Reaction Center Complex Proteins, Photosystem I, Photosystem II, Proton transfer, Rapid-scan FTIR, Reaction centers, Rhodobacter sphaeroides, Spectroscopy, Fourier Transform Infrared, Step-scan FTIR, Thylakoids, Ubiquinone, Vibrational spectroscopy.

  • D. Moonshiram, A. Picón, A. Vazquez-Mayagoitia, X. Zhang, M. - F. Tu, P. Garrido-Barros, J. - P. Mahy, F. Avenier, et A. Aukauloo, « Elucidating light-induced charge accumulation in an artificial analogue of methane monooxygenase enzymes using time-resolved X-ray absorption spectroscopy », Chemical Communications (Cambridge, England), vol. 53, nᵒ 18, p. 2725-2728, 2017.
    Résumé : We report the use of time-resolved X-ray absorption spectroscopy in the ns-μs time scale to track the light induced two electron transfer processes in a multi-component photocatalytic system, consisting of [Ru(bpy)3](2+)/ a diiron(iii,iii) model/triethylamine. EXAFS analysis with DFT calculations confirms the structural configurations of the diiron(iii,iii) and reduced diiron(ii,ii) states.
    Mots-clés : B3S, LPB.

  • D. Sorigué, B. Légeret, S. Cuiné, S. Blangy, S. Moulin, E. Billon, P. Richaud, S. Brugière, Y. Couté, D. Nurizzo, P. Müller, K. Brettel, D. Pignol, P. Arnoux, Y. Li-Beisson, G. Peltier, et F. Beisson, « An algal photoenzyme converts fatty acids to hydrocarbons », Science (New York, N.Y.), vol. 357, nᵒ 6354, p. 903-907, 2017.
    Résumé : Although many organisms capture or respond to sunlight, few enzymes are known to be driven by light. Among these are DNA photolyases and the photosynthetic reaction centers. Here, we show that the microalga Chlorella variabilis NC64A harbors a photoenzyme that acts in lipid metabolism. This enzyme belongs to an algae-specific clade of the glucose-methanol-choline oxidoreductase family and catalyzes the decarboxylation of free fatty acids to n-alkanes or -alkenes in response to blue light. Crystal structure of the protein reveals a fatty acid-binding site in a hydrophobic tunnel leading to the light-capturing flavin adenine dinucleotide (FAD) cofactor. The decarboxylation is initiated through electron abstraction from the fatty acid by the photoexcited FAD with a quantum yield >80%. This photoenzyme, which we name fatty acid photodecarboxylase, may be useful in light-driven, bio-based production of hydrocarbons.
    Mots-clés : B3S, LPB.

  • A. G. Tebo, A. Quaranta, C. Herrero, V. L. Pecoraro, et A. Aukauloo, « Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein », ChemPhotoChem, vol. 1, nᵒ 3, p. 89-92, 2017.
    Résumé : Long-distance biological electron transfer occurs through a hopping mechanism and often involves tyrosine as a high potential intermediate, for example in the early charge separation steps during photosynthesis. Protein design allows for the development of minimal systems to study the underlying principles of complex systems. Herein, we report the development of the first ruthenium-linked designed protein for the photogeneration of a tyrosine radical by intramolecular electron transfer.
    Mots-clés : B3S, Electron transfer, LPB, photochemistry, protein design, radicals, Tyrosine.


  • J. Yamamoto, P. Plaza, et K. Brettel, « Repair of (6-4) Lesions in DNA by (6-4) Photolyase: 20 Years of Quest for the Photoreaction Mechanism », Photochemistry and Photobiology, vol. 93, nᵒ 1, p. 51-66, 2017.

  • J. Yamamoto, K. Shimizu, T. Kanda, Y. Hosokawa, S. Iwai, P. Plaza, et P. Müller, « Loss of fourth electron-transferring tryptophan in animal (6-4) photolyase impairs DNA repair activity in bacterial cells », Biochemistry, 2017.
    Résumé : (6-4) photolyases ((6-4)PLs) are flavoproteins that use blue light to repair the UV-induced pyrimidine(6-4)pyrimidone photoproduct in DNA. Their FAD cofactor can be reduced to its repair-active FADH- form by a photoinduced electron transfer reaction. In animal (6-4)PLs, a chain of four Trp residues was suggested to be involved in a step-wise transfer of an oxidation hole from the flavin to the surface of the protein. Here, we investigated the effect of mutation of the fourth Trp on the DNA photorepair activity of Xenopus laevis (6-4)PL (Xl64) in bacterial cells. The photoreduction and photorepair properties of this mutant protein were independently characterized in vitro. Our results demonstrate that the mutation of the fourth Trp in Xl64 drastically impairs the DNA repair activity in cells, and that this effect is due to the inhibition of the photoreduction process. We thereby show that the photoreductive formation of FADH- through the Trp tetrad is essential for the biological function of the animal (6-4)PL. The role of the Trp cascade, and of the fourth Trp in particular, are discussed.
    Mots-clés : B3S, DC, LPB.

2016


  • F. Cailliez, P. Müller, T. Firmino, P. Pernot, et A. de la Lande, « Energetics of Photoinduced Charge Migration within the Tryptophan Tetrad of an Animal (6-4) Photolyase », Journal of the American Chemical Society, vol. 138, nᵒ 6, p. 1904-1915, 2016.
    Résumé : Cryptochromes and photolyases are flavoproteins that undergo cascades of electron/hole transfers after excitation of the flavin cofactor. It was recently discovered that animal (6-4) photolyases, as well as animal cryptochromes, feature a chain of four tryptophan residues, while other members of the family contain merely a tryptophan triad. Transient absorption spectroscopy measurements on Xenopus laevis (6-4) photolyase have shown that the fourth residue is effectively involved in photoreduction but at the same time could not unequivocally ascertain the final redox state of this residue. In this article, polarizable molecular dynamics simulations and constrained density functional theory calculations are carried out to reveal the energetics of charge migration along the tryptophan tetrad. Migration toward the fourth tryptophan is found to be thermodynamically favorable. Electron transfer mechanisms are sought either through an incoherent hopping mechanism or through a multiple sites tunneling process. The Jortner-Bixon formulation of electron transfer (ET) theory is employed to characterize the hopping mechanism. The interplay between electron transfer and relaxation of protein and solvent is analyzed in detail. Our simulations confirm that ET in (6-4) photolyase proceeds out of equilibrium. Multiple site tunneling is modeled with the recently proposed flickering resonance mechanism. Given the position of energy levels and the distribution of electronic coupling values, tunneling over three tryptophan residues may become competitive in some cases, although a hopping mechanism is likely to be the dominant channel. For both reactive channels, computed rates are very sensitive to the starting protein configuration, suggesting that both can take place and eventually be mixed, depending on the state of the system when photoexcitation takes place.
    Mots-clés : Animals, B3S, Deoxyribodipyrimidine Photo-Lyase, Electron Transport, LPB, Molecular Dynamics Simulation, Tryptophan.


  • K. Gibasiewicz, R. Białek, M. Pajzderska, J. Karolczak, G. Burdziński, M. R. Jones, et K. Brettel, « Weak temperature dependence of P + H A − recombination in mutant Rhodobacter sphaeroides reaction centers », Photosynthesis Research, vol. 128, nᵒ 3, p. 243-258, 2016.

  • P. Müller, K. Brettel, L. Grama, M. Nyitrai, et A. Lukacs, « Photochemistry of Wild-Type and N378D Mutant E. coli DNA Photolyase with Oxidized FAD Cofactor Studied by Transient Absorption Spectroscopy », Chemphyschem: A European Journal of Chemical Physics and Physical Chemistry, vol. 17, nᵒ 9, p. 1329-1340, 2016.
    Résumé : DNA photolyases (PLs) and evolutionarily related cryptochrome (CRY) blue-light receptors form a widespread superfamily of flavoproteins involved in DNA photorepair and signaling functions. They share a flavin adenine dinucleotide (FAD) cofactor and an electron-transfer (ET) chain composed typically of three tryptophan residues that connect the flavin to the protein surface. Four redox states of FAD are relevant for the various functions of PLs and CRYs: fully reduced FADH(-) (required for DNA photorepair), fully oxidized FADox (blue-light-absorbing dark state of CRYs), and the two semireduced radical states FAD(.-) and FADH(.) formed in ET reactions. The PL of Escherichia coli (EcPL) has been studied for a long time and is often used as a reference system; however, EcPL containing FADox has so far not been investigated on all relevant timescales. Herein, a detailed transient absorption study of EcPL on timescales from nanoseconds to seconds after excitation of FADox is presented. Wild-type EcPL and its N378D mutant, in which the asparagine facing the N5 of the FAD isoalloxazine is replaced by aspartic acid, known to protonate FAD(.-) (formed by ET from the tryptophan chain) in plant CRYs in about 1.5 μs, are characterized. Surprisingly, the mutant protein does not show this protonation. Instead, FAD(.-) is converted in 3.3 μs into a state with spectral features that are different from both FADH(.) and FAD(.-) . Such a conversion does not occur in wild-type EcPL. The chemical nature and formation mechanism of the atypical FAD radical in N378D mutant EcPL are discussed.
    Mots-clés : B3S, CPD photolyase, cryptochrome, Electron transfer, flavin radicals, LPB, Proton transfer.


  • J. S. Plegaria, C. Herrero, A. Quaranta, et V. L. Pecoraro, « Electron transfer activity of a de novo designed copper center in a three-helix bundle fold », Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1857, nᵒ 5, p. 522-530, 2016.

2015


  • J. - F. Cornet, A. Aukauloo, F. Gloaguen, et W. Leibl, « Ingénierie de la photosynthèse artificielle. Verrous et perspectives », L’actualité chimique, p. 69-74, 2015.
    Résumé : La photosynthèse artificielle est une voie prometteuse pour obtenir des carburants stockables à partir d’énergie solaire et d’eau, voire aussi de CO2. Sa mise en œuvre nécessitera néanmoins de surmonter de nombreux verrous, relevant autant de la chimie et de la physique fondamentales que de l’ingénierie. Cet article fait le point sur l’ensemble des problématiques concernées, de l’échelle moléculaire à l’échelle du procédé, de façon intégrée. Il examine sous quelles conditions des performances énergétiques et cinétiques élevées pourront un jour être atteintes et ouvrir ainsi la voie au déploiement industriel à grande échelle de ces procédés de conversion de l’énergie solaire.
    Mots-clés : B3S, LPB.

  • D. de Bellefeuille, M. Orio, A. - L. Barra, A. Aukauloo, Y. Journaux, C. Philouze, X. Ottenwaelder, et F. Thomas, « Redox noninnocence of the bridge in copper(II) salophen and bis(oxamato) complexes », Inorganic Chemistry, vol. 54, nᵒ 18, p. 9013-9026, 2015.
    Résumé : Two square-planar copper(II) complexes of 1,2-bis(2-hydroxy-3,5-di-tert-butylbenzimino)-4,5-bis(dimethylamino)benzene (1) and N-[4,5-bis(dimethylamino)-2-(oxalylamino)benzene]oxamate (2(2-)) were prepared. The crystal structures of the proligands H2L(1) and Et2H2L(2), as well as the corresponding complexes, are reported. The proligands each display a one-electron-oxidation wave, which is assigned to oxidation of the bis(dimethylamino)benzene moiety into a π radical. Complexes 1 and 2(2-) exhibit reversible one-electron-oxidation waves in their cyclic voltammograms (E1/2(1) = 0.14 and E1/2(2) = 0.31 V for 1 and E1/2(1) = -0.47 V vs Fc(+)/Fc for 2(2-)). The first process corresponds to oxidation of the bis(dimethylamino)benzene central ring into a π radical, while the second process for 1 is ascribed to oxidation of the π radical into an α-diiminoquinone. The one-electron-oxidized species 1(+) and 2(-) exhibit intense visible-near-IR absorptions, which are diagnostic of π radicals. They display a triplet signal in their electron paramagnetic resonance spectra, which stem from magnetic coupling between the ligand-radical spin and the copper(II) spin. The zero-field-splitting parameters are larger for 2(-) than 1(+) because of greater delocalization of the spin density onto the coordinated amidato N atoms. Density functional theory calculations support a π-radical nature of the one-electron-oxidized complexes, as well as S = 1 ground spin states. The electrogenerated 1(2+) comprises a closed-shell diiminoquinone ligand coordinated to a copper(II) metal center. Both 1 and 2 catalyze the aerobic oxidation of benzyl alcohol, albeit with different yields.
    Mots-clés : B3S, Benzyl Alcohol, Coordination Complexes, Copper, Electrochemistry, Electron Spin Resonance Spectroscopy, LPB, Molecular Structure, Oxamic Acid, Oxidation-Reduction, Salicylates.


  • C. Ducloiset, P. Jouin, E. Paredes, R. Guillot, M. Sircoglou, M. Orio, W. Leibl, et A. Aukauloo, « Monoanionic Dipyrrin-Pyridine Ligands: Synthesis, Structure and Photophysical Properties: Monoanionic Dipyrrin-Pyridine Ligands », European Journal of Inorganic Chemistry, vol. 2015, nᵒ 32, p. 5405-5410, 2015.


  • C. Herrero, A. Quaranta, M. Sircoglou, K. Sénéchal-David, A. Baron, I. M. Marín, C. Buron, J. - P. Baltaze, W. Leibl, A. Aukauloo, et F. Banse, « Successive light-induced two electron transfers in a Ru–Fe supramolecular assembly: from Ru–Fe(II)–OH2 to Ru–Fe(IV)–oxo », Chem. Sci., vol. 6, nᵒ 4, p. 2323-2327, 2015.


  • M. Malferrari, P. Turina, F. Francia, A. Mezzetti, W. Leibl, et G. Venturoli, « Dehydration affects the electronic structure of the primary electron donor in bacterial photosynthetic reaction centers: evidence from visible-NIR and light-induced difference FTIR spectroscopy », Photochem. Photobiol. Sci., vol. 14, nᵒ 2, p. 238-251, 2015.

  • P. Müller et J. - P. Bouly, « Searching for the mechanism of signalling by plant photoreceptor cryptochrome », FEBS letters, vol. 589, nᵒ 2, p. 189-192, 2015.
    Résumé : Even though the plant photoreceptors cryptochromes were discovered more than 20 years ago, the mechanism through which they transduce light signals to their partner molecules such as COP1 (Constitutive Photomorphogenic 1) or SPA1 (Suppressor of Phytochrome A) still remains to be established. We propose that a negative charge induced by light in the vicinity of the flavin chromophore initiates cryptochrome 1 signalling. This negative charge might expel the protein-bound ATP from the binding pocket, thereby pushing off the C-terminus that covers the ATP pocket in the dark state of the protein. This conformational change should allow for phosphorylation of previously inaccessible amino acids. A partially phosphorylated 'ESSSSGRR-VPE' fragment of the C-terminus could mimic the sequence of the transcription factor HY5 that is essential for binding to the negative regulator of photomorphogenesis COP1. HY5 release through competition for the COP1 binding site could represent the long-sought connection between light activation of cryptochrome and modulation of photomorphogenesis.
    Mots-clés : ATP, B3S, Constitutive Photomorphogenic 1, Cryptochromes, HY5, LPB, Photoreceptor, Plant cryptochrome, Plant Proteins, Plants, Protein Binding, Signal Transduction, Signalling, Transcription Factors.


  • P. Müller, J. Yamamoto, R. Martin, S. Iwai, et K. Brettel, « Discovery and functional analysis of a 4th electron-transferring tryptophan conserved exclusively in animal cryptochromes and (6-4) photolyases », Chem. Commun., vol. 51, nᵒ 85, p. 15502-15505, 2015.

  • C. Orain, L. Saujet, C. Gauquelin, P. Soucaille, I. Meynial-Salles, C. Baffert, V. Fourmond, H. Bottin, et C. Léger, « Electrochemical Measurements of the Kinetics of Inhibition of Two FeFe Hydrogenases by O2 Demonstrate That the Reaction Is Partly Reversible », Journal of the American Chemical Society, vol. 137, nᵒ 39, p. 12580-12587, 2015.
    Résumé : The mechanism of reaction of FeFe hydrogenases with oxygen has been debated. It is complex, apparently very dependent on the details of the protein structure, and difficult to study using conventional kinetic techniques. Here we build on our recent work on the anaerobic inactivation of the enzyme [Fourmond et al. Nat. Chem. 2014, 4, 336-342] to propose and apply a new method for studying this reaction. Using electrochemical measurements of the turnover rate of hydrogenase, we could resolve the first steps of the inhibition reaction and accurately determine their rates. We show that the two most studied FeFe hydrogenases, from Chlamydomonas reinhardtii and Clostridium acetobutylicum, react with O2 according to the same mechanism, despite the fact that the former is much more O2 sensitive than the latter. Unlike often assumed, both enzymes are reversibly inhibited by a short exposure to O2. This will have to be considered to elucidate the mechanism of inhibition, before any prediction can be made regarding which mutations will improve oxygen resistance. We hope that the approach described herein will prove useful in this respect.
    Mots-clés : B3S, Catalytic Domain, Electrochemistry, Hydrogenase, Iron-Sulfur Proteins, Kinetics, LPB, Models, Molecular, Oxygen.

  • A. Quaranta, G. Charalambidis, C. Herrero, S. Margiola, W. Leibl, A. Coutsolelos, et A. Aukauloo, « Synergistic "ping-pong" energy transfer for efficient light activation in a chromophore-catalyst dyad », Physical chemistry chemical physics: PCCP, vol. 17, nᵒ 37, p. 24166-24172, 2015.
    Résumé : The synthesis of a porphyrin-Ru(II) polypyridine complex where the porphyrin acts as a photoactive unit and the Ru(II) polypyridine as a catalytic precursor is described. Comparatively, the free base porphyrin was found to outperform the ruthenium based chromophore in the yield of light induced electron transfer. Mechanistic insights indicate the occurrence of a ping-pong energy transfer from the (1)LC excited state of the porphyrin chromophore to the (3)MCLT state of the catalyst and back to the (3)LC excited state of the porphyrin unit. The latter, triplet-triplet energy transfer back to the chromophore, efficiently competes with fast radiationless deactivation of the excited state at the catalyst site. The energy thus recovered by the chromophore allows improved yield of formation of the oxidized form of the chromophore and concomitantly of the oxidation of the catalytic unit by intramolecular charge transfer. The presented results are among the rare examples where a porphyrin chromophore is successfully used to drive an oxidative activation process where reductive processes prevail in the literature.
    Mots-clés : B3S, Catalysis, Energy Transfer, Light, LPB, Molecular Structure, Organometallic Compounds, Porphyrins, Pyridines, Ruthenium.

  • L. Schneider, Y. Mekmouche, P. Rousselot-Pailley, A. J. Simaan, V. Robert, M. Réglier, A. Aukauloo, et T. Tron, « Visible-Light-Driven Oxidation of Organic Substrates with Dioxygen Mediated by a [Ru(bpy)3 ](2+) /Laccase System », ChemSusChem, vol. 8, nᵒ 18, p. 3048-3051, 2015.
    Résumé : Oxidation reactions are highly important chemical transformations that still require harsh reaction conditions and stoichiometric amounts of chemical oxidants that are often toxic. To circumvent these issues, olefins oxidation is achieved in mild conditions upon irradiation of an aqueous solution of the complex [Ru(bpy)3 ](2+) and the enzyme laccase. Epoxide formation is coupled to the light-driven reduction of O2 by [Ru(bpy)3 ](2+) /laccase system. The reactivity can be explained by dioxygen acting both as an oxidative agent and as renewable electron acceptor, avoiding the use of a sacrificial electron acceptor.
    Mots-clés : Alkenes, B3S, Copper, enzyme catalysis, Epoxy Compounds, Laccase, Light, LPB, Models, Molecular, olefins, Organometallic Compounds, Oxidants, oxidation, Oxidation-Reduction, Oxygen, Photochemical Processes, Protein Conformation, Ruthenium.
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Publications majeures avant 2015

-  Avenier F, Herrero C, Leibl W, Desbois A, Guillot R, Mahy JP, Aukauloo A (2013) Photoassisted Generation of a Dinuclear Iron(III) Peroxo Species Leading to Oxygen Atom Transfer Reaction
Angew. Chemie Int. Ed. 52, 3634-3637.

-  Herrero C, Costentin C, Aukauloo A (2011) Converting Photons to Electron and Proton Shifts from Water for Fuel Production. Molecular Solar Fuels. RSC Press, 39-84.

-  Herrero C, Batchelor L, Baron A, El Ghachtouli S, Sheth S, Guillot R, Vauzeilles B, Sircoglou M, Mallah T, Leibl W, Aukauloo A (2012) Click Chemistry as a Convenient Tool for the Incorporation of a Ruthenium Chromophore and a Nickel–Salen Monomer into a Visible-Light-Active Assembly. European Journal of Inorganic Chemistry, 2013, 494-499.

-  Baron A, Herrero C, Quaranta A, Leibl W, Vauzeilles B, Aukauloo A (2012) An efficient and versatile synthetic route for photoactive modular assemblies. Inorg. Chem. 51, 5985-5987.

-  Baron A, Herrero C, Quaranta A, Charlot MF, Leibl W, Vauzeilles B, Aukauloo A (2011) Efficient electron transfer through a triazole link in ruthenium(II) polypyridine type complexes. Chem. Comm. 47, 11011-11013.

-  Herrero C, Quaranta A, Leibl W, Rutherford AW, Aukauloo A (2011) Artificial photosynthetic systems. Using light and water to provide electrons and protons for the synthesis of a fuel. Energy and Environmental Chemistry 4, 2353-2365.

-  Herrero C, Quaranta A, Protti S, Leibl W, Rutherford AW, Fallahpour R, Charlot MF, Aukauloo A (2011) Light driven activation of the [H2O(terpy)MnIII-di-µ-oxo-MnIV(terpy)OH2] unit in a chromophore-catalyst complex. Chem. Asian J. 6 : 1335–1339

-  Herrero C, Hughes JL, Quaranta A, Cox N, Rutherford AW, Leibl W, Aukauloo A (2010) Intramolecular Light Induced Activation of a Salen-Mn(III) Complex by a Ruthenium Photosensitizer. Chemical Communications 46, 7605-7607.

-  Mezzetti A, Blanchet L, de Juan A, Leibl W, Ruckebusch C (2010) Ubiquinol formation in isolated photosynthetic reaction centers monitored by time-resolved differential FTIR in combination with 2D correlation spectroscopy and multivariate curve resolution. Anal. Bioanal. Chemistry, 399, 1999-2014.

-  Herrero C, Lassalle-Kaiser B, Leibl W, Rutherford AW, Aukauloo A (2008) Artificial systems related to light driven electron transfer processes in PSII. Coordination Chemistry Reviews 252, 456-468.

-  Fihri A, Artero A, Razavet M, Baffert C, Leibl W, Fontecave M (2008) Cobaloxime-Based Photocatalytic Devices for Hydrogen Production. Angew. Chemie Int. Ed. 47, 564–567.

-  Sybirna K, Ezanno P, Baffert C, Léger C, Bottin H (2013) Arginine171 of Chlamydomonas reinhardtii [Fe-Fe] hydrogenase HydA1 plays a crucial role in the electron transfer to its catalytic center. Int. Journal of Hydrogen Energy. http://dx.doi.org/10.1016/j.ijhydene.2012.12.078

-  Baffert C, Sybirna K, Ezanno P, Lautier T, Hajj V, Meynial-Salles I, Soucaille P, Bottin H, Léger C (2012) Covalent Attachment of FeFe Hydrogenases to Carbon Electrodes for Direct Electron Transfer. Analytical Chemistry 84, 7999-8005.

-  Dutheil J., Saenkham P., Sakr S., Leplat C., Ortega-Ramos M., Bottin H., Cournac L., Cassier-Chauvat C., Chauvat F. (2012) The AbrB2 Autorepressor, Expressed from an Atypical Promoter, Represses the Hydrogenase Operon To Regulate Hydrogen Production in Synechocystis Strain PCC6803. Journal Of Bacteriology 194, 5423-5433.

-  Baffert C., Bertini L., Lautier T., Greco C., Sybirna K., Ezanno P., Etienne E., Soucaille P., Bertrand P., Bottin H., Meynial-Salles I., De Gioia L., Leger C.( 2011) CO Disrupts the Reduced H-Cluster of FeFe Hydrogenase. A Combined DFT and Protein Film Voltammetry Study. Journal Of The American Chemical Society 133, 2096-2099.

-  Shi L., Belchik S.M., Plymale A.E., Heald S., Dohnalkova A.C., Sybirna K., Bottin H., Squier T.C., Zachara J.M., Fredrickson J.K. (2011) Purification and Characterization of the [NiFe]-Hydrogenase of Shewanella oneidensis MR-1. Applied And Environmental Microbiology 77, 5584-5590.

-  Sybirna K., Antoine T., Lindberg P., Fourmond V., Rousset M., Mejean V., Bottin H. (2008) Shewanella oneidensis : a new and efficient system for expression and maturation of heterologous [Fe-Fe] hydrogenase from Chlamydomonas reinhardtii. Bmc Biotechnology 8.

-  Byrdin M, Villette S, Espagne A, Eker APM, Brettel K (2008) Polarized Transient Absorption To Resolve Electron Transfer between Tryptophans in DNA Photolyase. J Phys Chem B 112, 6866–6871.

-  Lukacs A, Eker APM, Byrdin M, Brettel K, Vos MH (2008) Electron Hopping through the 15 Å Triple Tryptophan Molecular Wire in DNA Photolyase Occurs within 30 ps. J Am Chem Soc 130, 14394-14395.

-  Byrdin M, Thiagarajan V, Villette S, Espagne A, Brettel K (2009) Use of ruthenium dyes for subnanosecond detector fidelity testing in real time transient absorption. Rev Sci Instrum 80, 043102.

-  Balland V, Byrdin M, Eker APM, Ahmad M, Brettel K (2009) What makes the difference between a cryptochrome and DNA photolyase ? A spectroelectrochemical comparison of the flavin redox transitions. J Am Chem Soc 131, 426-427.

-  Espagne A, Byrdin M, Eker APM, Brettel K (2009) Very Fast Product Release and Catalytic Turnover of DNA Photolyase. ChemBioChem 10, 1777-1780.

-  Byrdin M, Lukacs A, Thiagarajan V, Eker APM, Brettel K, Vos MH (2010) Quantum yield measurements of short-lived photoactivation intermediates in DNA photolyase : Toward a detailed understanding of the triple tryptophan electron transfer chain. J Phys Chem A 114, 3207–3214.

-  Thiagarajan V, Villette S, Espagne A, Eker APM, Brettel K, Byrdin M (2010) DNA repair by photolyase : A novel substrate with low background absorption around 265 nm for transient absorption studies in the UV. Biochemistry 49, 297-303.

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