Research Topics
| Marten H VosSummaryAffiliation: Ecole Polytechnique Country: France Publications
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Detail Information
Publications
Ultrafast dynamics of ligands within heme proteinsMarten H Vos
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau, France
Biochim Biophys Acta 1777:15-31. 2008..In this review, an overview is given of recent progress in this field, and in particular on initial sensing processes in signaling proteins, and on ligand and electron transfer dynamics in oxidases and cytochromes...
Ultrafast ligand dynamics in the heme-based GAF sensor domains of the histidine kinases DosS and DosT from Mycobacterium tuberculosisMarten H Vos
Laboratory for Optics and Biosciences, CNRS Ecole Polytechnique, 91128 Palaiseau, France
Biochemistry 51:159-66. 2012..The distal tyrosine, present in both proteins, plays an important role in these processes...
Ultrafast heme-residue bond formation in six-coordinate heme proteins: implications for functional ligand exchangeMarten H Vos
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau, France
Biochemistry 47:5718-23. 2008..to functionally replace the internal residue after thermal dissociation of the heme-residue bond...- Strong ligand-protein interactions revealed by ultrafast infrared spectroscopy of CO in the heme pocket of the oxygen sensor FixLPatrick Nuernberger
Laboratoire d Optique et Biosciences, Ecole Polytechnique, CNRS, 91128 Palaiseau, France
J Am Chem Soc 133:17110-3. 2011.... - Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensorsMichel Negrerie
INSERM U696, Laboratoire d Optique et Biosciences, Ecole Polytechnique, Palaiseau F91120, 91128 Palaiseau Cedex, France
J Biol Chem 281:10389-98. 2006..Consequently, the heme coordination state together with the energy barriers provided by the protein structure control the dynamics and affinity for NO-binding enzymes... - Direct observation of ligand transfer and bond formation in cytochrome c oxidase by using mid-infrared chirped-pulse upconversionJohanne Treuffet
Laboratoire d Optique et Biosciences, Ecole Polytechnique, Centre National de la Recherche Scientifique and Institut National de la Santé et de la Recherche Médicale U696, 91128 Palaiseau, France
Proc Natl Acad Sci U S A 104:15705-10. 2007..Both experimental and calculated data strongly suggest a ballistic contribution to the transfer process... - Role of distal arginine in early sensing intermediates in the heme domain of the oxygen sensor FixLAudrius Jasaitis
CNRS, UMR 7645, Laboratory for Optical Biosciences, Ecole Polytechnique, 91128 Palaiseau Cedex, France
Biochemistry 45:6018-26. 2006..Molecular dynamics simulations corroborate these findings and suggest motions of O(2) and arginine 220 away from the heme pocket as a second step in the signal pathway on the 50 ps time scale... - Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopySergei G Kruglik
Laboratoire d Optique et Biosciences, Centre National de la Recherche, Ecole Polytechnique, 91128 Palaiseau Cedex, France
Proc Natl Acad Sci U S A 104:7408-13. 2007..These results uncover the origin of the "oxygen cage" properties of this oxygen sensor protein... - Ligand dynamics and early signaling events in the heme domain of the sensor protein Dos from Escherichia coliTaku Yamashita
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau and INSERM U696, F 91128 Palaiseau, France
J Biol Chem 283:2344-52. 2008..We suggest that this configuration corresponds to an early signaling intermediate state, is responsible for the slow rebinding, and allows small ligands in the protein to efficiently compete for binding with the heme... - Ultrafast ligand binding dynamics in the active site of native bacterial nitric oxide reductaseSofia M Kapetanaki
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau, France INSERM U696, F 91128 Palaiseau, France
Biochim Biophys Acta 1777:919-24. 2008..Our results reveal that heme-ligand recombination in this enzyme is considerably faster than in heme-copper oxidases and are consistent with a more confined configuration of the active site... - Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteinsSergei G Kruglik
Laboratoire d Optique et Biosciences, Institut National de la Sante et de la Recherche Medicale, Ecole Polytechnique, 91128 Palaiseau, France
Proc Natl Acad Sci U S A 107:13678-83. 2010..This observed phenomenon constitutes the primary structural transition in heme proteins induced by NO binding... - Nanosecond electron tunneling between the hemes in cytochrome bo3Audrius Jasaitis
Laboratoire d Optique et Biosciences, Centre National de la Recherche Scientifique, Ecole Polytechnique, 91128 Palaiseau, France
Proc Natl Acad Sci U S A 104:20811-4. 2007..The properties of eT between the closely lying heme groups in the heme-copper oxidases are discussed in terms of the reorganization energy for the process, and two methods for assessing the rate of electron tunneling are presented... - Ultrafast heme dynamics in ferrous versus ferric cytochrome c studied by time-resolved resonance Raman and transient absorption spectroscopyMichel Negrerie
Laboratory for Optics and Biosciences, CNRS UMR 7645, Ecole Polytechnique, 91128 Palaiseau Cedex, France
J Phys Chem B 110:12766-81. 2006.... - Accommodation of NO in the active site of mammalian and bacterial cytochrome c oxidase aa3Eric Pilet
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau cedex, France
Biochim Biophys Acta 1767:387-92. 2007..The unexpected differences highlighted in this study may relate to differences in the physiological relevance of the CcO-NO interactions in both species... - Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complexSofia M Kapetanaki
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, and INSERM U696, F 91128 Palaiseau, France
Biochemistry 48:1613-9. 2009..and Wallace, C. J. A. (2007) Biochem. J. 407, 179-187]. The affinity of CO for the complex is high enough to envisage an antiapoptotic effect of nanomolar CO concentrations via inhibition of the cyt c peroxidase activity... - Electron transfer between hemes in mammalian cytochrome c oxidaseEric Pilet
, Centre National de la Recherche Scientifique, , Ecole Polytechnique, , 91128 Palaiseau Cedex, France
Proc Natl Acad Sci U S A 101:16198-203. 2004..We discuss the potential physiological relevance of fast equilibration associated with this low-driving-force redox reaction... - Vibrational motions associated with primary processes in bacteriorhodopsin studied by coherent infrared emission spectroscopyGeza I Groma
Laboratory for Optical Biosciences, Ecole Polytechnique, Institut National de la Sante et de la Recherche Medicale, Centre National de la Recherche Scientifique, Palaiseau, France
Biophys J 100:1578-86. 2011..In particular, the direction sensitivity provides experimental evidence for large intermediate distortions of the retinal plane during the excited-state isomerization process... - Suppression of perturbed free-induction decay and noise in experimental ultrafast pump-probe dataPatrick Nuernberger
Laboratoire d Optique et Biosciences, Ecole Polytechnique, CNRS, France
Opt Lett 34:3226-8. 2009..We demonstrate these filters using visible pump/mid-infrared probe spectroscopy of ligand dissociation in carboxyhemoglobin... - Nitric oxide (NO) traffic in endothelial NO synthase. Evidence for a new NO binding site dependent on tetrahydrobiopterin?Anny Slama-Schwok
Laboratory for Optics and Biosciences, INSERM U451, CNRS Unite Mixte de Recherche 7645, Ecole Polytechnique, 91128 Palaiseau, France
J Biol Chem 277:7581-6. 2002..The new non-heme site may act as a "doorstep" to the heme pocket and control NO escape from eNOS... - Photodissociation of heme distal methionine in ferrous cytochrome C revealed by subpicosecond time-resolved resonance Raman spectroscopySimona Cianetti
Laboratory for Optics and Biosciences, INSERM U451, CNRS UMR 7645, Ecole Polytechnique, 91128 Palaiseau Cedex, France
J Am Chem Soc 126:13932-3. 2004.... - Electron hopping through the 15 A triple tryptophan molecular wire in DNA photolyase occurs within 30 psAndras Lukacs
Laboratoire d Optique et Biosciences, CNRS, Ecole Polytechnique, F 91128 Palaiseau, France
J Am Chem Soc 130:14394-5. 2008..In DNA photolyase we make use of the natural photoactivation of the process, but more generally chains of aromatic amino acids may allow very fast long-range electron transfer also in nonphotoactive proteins... - Quantification of sudden light-induced polarization in bacteriorhodopsin by optical rectificationAnne Colonna
Laboratory for Optical Biosciences, Ecole Polytechnique, INSERM, CNRS, 91128 Palaiseau, France
J Phys Chem B 111:2707-10. 2007..This result may help to evaluate models describing the interplay between the initial polarization change and the subsequent isomerization of the retinal... - Ligand binding dynamics to the heme domain of the oxygen sensor Dos from Escherichia coliUrsula Liebl
Laboratory for Optical Biosciences, INSERM U451, CNRS UMR 7645, Ecole Polytechnique ENSTA, 91128 Palaiseau Cedex, France
Biochemistry 42:6527-35. 2003..Further remarkable observations include evidence for stable (>4 ns) photooxidation of six-coordinate ferrous heme, with a quantum yield of 4-8%... - Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: general regulatory implications for heme-based sensorsUrsula Liebl
Laboratory for Optical Biosciences, Institut National de la Santé et de la Recherche Médicale U451, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7645, France
Proc Natl Acad Sci U S A 99:12771-6. 2002..The general implications for the functioning of heme-based ligand sensors are discussed in the light of recent studies on heme-based NO and CO sensors... - Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome cGary Silkstone
Department of Biological Sciences, Wivenhoe Park, University of Essex, Colchester CO4 3SQ, United Kingdom
J Biol Chem 282:1638-49. 2007..Experiments on double mutants in which Phe-82 is replaced by Asp or Gly as well as the M80D substitution indicate that such steric changes substantially increase the motional freedom-dissociated CO... - Role of arginine 220 in the oxygen sensor FixL from Bradyrhizobium japonicumVeronique Balland
Laboratoire de Biophysique du Stress Oxydant, SBE DBJC and CNRS URA 2096, CEA Saclay, 91191 Gif sur Yvette Cedex, France
J Biol Chem 280:15279-88. 2005.... - Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopyVitaliy B Borisov
A N Belozersky Institute of Physico Chemical Biology, Moscow State University, Moscow 119899, Russia
Biochemistry 41:1654-62. 2002..In contrast to other known heme proteins, molecular oxygen cannot be photodissociated from the mixed-valence cytochrome bd at all, indicating a unique structural and electronic configuration of the diheme active site in the enzyme... - Hydrophobic distal pocket affects NO-heme geminate recombination dynamics in dehaloperoxidase and H64V myoglobinStefan Franzen
Department of Chemistry, North Carolina State University, Raleigh, NC 27695, USA
J Phys Chem B 110:14483-93. 2006..Both phenomena are similar to the effect of viscosity on wild-type Mb due to slowing of protein relaxation resulting from an increased solution viscosity and protein surface dehydration... - Dissection of the triple tryptophan electron transfer chain in Escherichia coli DNA photolyase: Trp382 is the primary donor in photoactivationMartin Byrdin
Service de Bioenergetique, Departement de Biologie Joliot Curie, Commissariat a l Energie Atomique, and Unité de Recherche Associée 2096, Centre National de la Recherche Scientifique, CEA Saclay, 91191 Gif sur Yvette Cedex, France
Proc Natl Acad Sci U S A 100:8676-81. 2003..The rate constants of electron transfer from W382 to excited FADH* in WT and from W359 to excited FADH* in W382F mutant photolyase were estimated and related to the donor-acceptor distances... - Coherent infrared emission from myoglobin crystals: an electric field measurementMarie-Louise Groot
Laboratory for Optical Biosciences, INSERM U451, , , 91128 Palaiseau Cedex, France
Proc Natl Acad Sci U S A 99:1323-8. 2002..The few deviations from this behavior in Mb-CO we propose are the result of these modes being sensitive to the photodissociation process and severely disrupted by it... - Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: review and new insights from an "inverse" deuterium isotope effectMartin Byrdin
Service de Bioenergetique, CEA, and URA 2096 CNRS, CEA Saclay, Bat 532, F 91191 Gif sur Yvette Cedex, France
Biochim Biophys Acta 1655:64-70. 2004.... - Resonant optical rectification in bacteriorhodopsinGeza I Groma
Institute of Biophysics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, H 6726, Hungary
Proc Natl Acad Sci U S A 101:7971-5. 2004..The simultaneous and phase-sensitive observation of both the electronic and vibrational signals opens the way to study the transduction of the initial polarization into structural dynamics... - Coherent vibrational climbing in carboxyhemoglobinCathie Ventalon
, , , Palaiseau, France
Proc Natl Acad Sci U S A 101:13216-20. 2004.... - NO binding and dynamics in reduced heme-copper oxidases aa3 from Paracoccus denitrificans and ba3 from Thermus thermophilusEric Pilet
Laboratory for Optical Biosciences, INSERM U451, CNRS UMR 7645, Ecole Polytechnique-ENSTA, 91128 Palaiseau Cedex, France
Biochemistry 43:14118-27. 2004..This proposal is supported by molecular-modeling studies that indicate a approximately 63 degrees rotation of heme-bound NO upon binding of a second NO to the close-lying copper center CuB. It is argued that the second NO binds to CuB... - Activationless electron transfer through the hydrophobic core of cytochrome c oxidaseAudrius Jasaitis
Laboratory for Optical Biosciences, INSERM U696, Centre National de la Recherche Scientifique, , , 91128 Palaiseau Cedex, France
Proc Natl Acad Sci U S A 102:10882-6. 2005..We discuss that low-DeltaG, low-lambda reactions are common for efficiently channeling electrons through chains that are buried inside membrane proteins... - Role of the middle residue in the triple tryptophan electron transfer chain of DNA photolyase: ultrafast spectroscopy of a Trp-->Phe mutantAndras Lukacs
J Phys Chem B 110:15654-8. 2006..Our results provide a first experimental indication that electron transfer between aromatic residues can take place on the time scale of approximately 10(-12) s...