S Gas Biology, Antioxidants & Redox Signaling, vol.13, issue.2, pp.157-92, 2010. ,
DOI : 10.1089/ars.2009.2657
Primary processes in heme-based sensor proteins, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1834, issue.9 ,
DOI : 10.1016/j.bbapap.2013.02.025
URL : https://hal.archives-ouvertes.fr/hal-00817153
Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.1-22, 2005. ,
DOI : 10.1016/j.jinorgbio.2004.11.006
Environmental Heme-Based Sensor Proteins: Implications for Understanding Bacterial Pathogenesis, Antioxidants & Redox Signaling, vol.17, issue.9, pp.1232-1277, 2012. ,
DOI : 10.1089/ars.2012.4613
Etude des hémoprotéines senseursàsenseursà oxygène bactériens FixL et Dos, 2006. ,
Novel Bacterial Gas Sensor Proteins with Transition Metal???Containing Prosthetic Groups as Active Sites, Antioxidants & Redox Signaling, vol.16, issue.7, pp.678-86, 2012. ,
DOI : 10.1089/ars.2011.4248
Ortiz de Montellano. 2.3 x-ray structure of the heme-bound gaf domain of sensory histidine kinase dost of Mycobacterium tuberculosis, Biochem, issue.47, pp.4712523-12531, 2008. ,
Structure of the Oxygen Sensor in Bacillus subtilis, Structure, vol.11, issue.9, pp.1097-1110, 2003. ,
DOI : 10.1016/S0969-2126(03)00169-2
High-resolution Crystal Structures of Two Polymorphs of Cytochromec??? from the Purple Phototrophic BacteriumRhodobacter capsulatus, Journal of Molecular Biology, vol.259, issue.3, pp.467-479, 1996. ,
DOI : 10.1006/jmbi.1996.0333
The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development, Cell, vol.67, issue.6, pp.671157-1167, 1991. ,
DOI : 10.1016/0092-8674(91)90292-7
The Oxygen Sensor Protein, FixL, of Rhizobium meliloti: ROLE OF HISTIDINE RESIDUES IN HEME BINDING, PHOSPHORYLATION, AND SIGNAL TRANSDUCTION, Journal of Biological Chemistry, vol.270, issue.10, pp.5243-5250, 1995. ,
DOI : 10.1074/jbc.270.10.5243
Heme-Based Sensors, Exemplified by the Kinase FixL, Are a New Class of Heme Protein with Distinctive Ligand Binding and Autoxidation, Biochemistry, vol.33, issue.26, pp.338067-73, 1994. ,
DOI : 10.1021/bi00192a011
Ultrafast dynamics of ligands within heme proteins, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1777, issue.1 ,
DOI : 10.1016/j.bbabio.2007.10.004
URL : https://hal.archives-ouvertes.fr/hal-00324230
Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance raman spectroscopic studies, Journal of Molecular Biology, vol.301, issue.2, pp.415-431, 2000. ,
DOI : 10.1006/jmbi.2000.3954
Characterization of a Direct Oxygen Sensor Heme Protein from Escherichia coli. EFFECTS OF THE HEME REDOX STATES AND MUTATIONS AT THE HEME-BINDING SITE ON CATALYSIS AND STRUCTURE, Journal of Biological Chemistry, vol.277, issue.26, pp.27723821-23827, 2002. ,
DOI : 10.1074/jbc.M202738200
An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for C-di-GMP control, Biochem, vol.48, issue.41, pp.9764-74, 2009. ,
Heme Sensor Proteins, Journal of Biological Chemistry, vol.288, issue.19, pp.13194-13203, 2013. ,
DOI : 10.1074/jbc.R112.422642
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3650359
A Novel Heme Protein That Acts as a Carbon Monoxide-Dependent Transcriptional Activator inRhodospirillum rubrum, Biochemical and Biophysical Research Communications, vol.228, issue.3, pp.752-756, 1996. ,
DOI : 10.1006/bbrc.1996.1727
Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators., Journal of Bacteriology, vol.177, issue.8, pp.1772157-63, 1995. ,
DOI : 10.1128/jb.177.8.2157-2163.1995
Myoglobin-like aerotaxis transducers in archaea and bacteria, Nature, vol.403, pp.540-544, 2000. ,
Guanylate cyclase and the ???NO/cGMP signaling pathway, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1411, issue.2-3, pp.334-350, 1999. ,
DOI : 10.1016/S0005-2728(99)00024-9
CooA, a paradigm for gas sensing regulatory proteins, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.280-92, 2005. ,
DOI : 10.1016/j.jinorgbio.2004.10.032
Heme Environmental Structure of CooA Is Modulated by the Target DNA Binding: EVIDENCE FROM RESONANCE RAMAN SPECTROSCOPY AND CO REBINDING KINETICS, Journal of Biological Chemistry, vol.273, issue.32, pp.27319988-19992, 1998. ,
DOI : 10.1074/jbc.273.32.19988
Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA, Acta Crystallographica Section D Biological Crystallography, vol.63, issue.3, pp.282-289, 2007. ,
DOI : 10.1107/S0907444906051638
Dissociation and Recombination between Ligands and Heme in a CO-sensing Transcriptional Activator CooA. A FLASH PHOTOLYSIS STUDY, Journal of Biological Chemistry, vol.275, issue.49 ,
DOI : 10.1074/jbc.M005533200
Ultrafast Heme???Residue Bond Formation in Six-Coordinate Heme Proteins: Implications for Functional Ligand Exchange, Biochemistry, vol.47, issue.21, pp.475718-475741, 2008. ,
DOI : 10.1021/bi800288z
URL : https://hal.archives-ouvertes.fr/inserm-00292529
Ligand Dynamics and Early Signaling Events in the Heme Domain of the Sensor Protein Dos from Escherichia coli, Journal of Biological Chemistry, vol.283, issue.4, pp.2344-2352, 2008. ,
DOI : 10.1074/jbc.M708123200
URL : https://hal.archives-ouvertes.fr/hal-00824267
NO sensing in Pseudomonas aeruginosa: Structure of the Transcriptional Regulator DNR, Journal of Molecular Biology, vol.378, issue.5, pp.1002-1017, 2008. ,
DOI : 10.1016/j.jmb.2008.03.013
. Crystal structure of wild-type DNR, Proteins: Structure, Function, and Bioinformatics, vol.283, issue.Pt 3, pp.174-180, 2009. ,
DOI : 10.1002/prot.22428
Unusual Heme Binding Properties of the Dissimilative Nitrate Respiration Regulator, a Bacterial Nitric Oxide Sensor, Antioxidants & Redox Signaling, vol.17, issue.9 ,
DOI : 10.1089/ars.2011.4226
URL : https://hal.archives-ouvertes.fr/pasteur-00952196
Study of the Zn-porphyrin structure by fluorescence spectroscopy methods, Journal of Applied Spectroscopy, vol.154, issue.4, pp.613-616, 1999. ,
DOI : 10.1007/BF02675396
A F??rster-resonance-energy transfer-based method for fluorescence detection of the protein redox state, Analytical Biochemistry, vol.350, issue.1, pp.52-60, 2006. ,
DOI : 10.1016/j.ab.2005.11.036
[19] Femtosecond measurements of geminate recombination in heme proteins, Hemoglobins Part C: Biophysical Methods, pp.416-430, 1994. ,
DOI : 10.1016/0076-6879(94)32057-8
and the Vibrational Relaxation of the Six-Coordinate Heme Species, Journal of the American Chemical Society, vol.124, issue.20, pp.5914-5938, 2002. ,
DOI : 10.1021/ja017359n
Photodissociation of heme distal methionine in ferrous cytochrome c revealed by subpicosecond time-resolved resonance Raman spectroscopy, J. Am. Chem. Soc, issue.43, pp.12613932-13933, 2004. ,
URL : https://hal.archives-ouvertes.fr/hal-00836427
Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy, Proceedings of the National Academy of Sciences, vol.104, issue.18 ,
DOI : 10.1073/pnas.0700445104
URL : https://hal.archives-ouvertes.fr/hal-00144493
Femtosecond processes in proteins, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1411, issue.1, pp.1-20, 1999. ,
DOI : 10.1016/S0005-2728(99)00035-3
Ligand binding dynamics to the Heme domain of the oxygen sensor Dos from Escherichia coli, Biochem, issue.21, pp.426527-6535, 2003. ,
URL : https://hal.archives-ouvertes.fr/hal-00836433
Electron transfer between hemes in mammalian cytochrome c oxidase, Proc. Natl. Acad. Sci, pp.16198-16203, 2004. ,
DOI : 10.1073/pnas.0405032101
URL : https://hal.archives-ouvertes.fr/hal-00831841
Principles of Fluorescence Spectroscopy, 2010. ,
DOI : 10.1007/978-0-387-46312-4
Trends in fluorescence imaging and related techniques to unravel biological information, HFSP Journal, vol.1, issue.3, pp.169-80, 2007. ,
DOI : 10.2976/1.2778852
Practical Course Biophyisics: Absorption and Fluorescence Spectroscopy ,
Fluorescence lifetime-based sensing and imaging, Sensors and Actuators B: Chemical, vol.29, issue.1-3, pp.16-24, 1995. ,
DOI : 10.1016/0925-4005(95)01658-9
Design and Characterization of a Femtosecond Fluorescence Spectrometer Based on Optical Kerr Gating, Applied Spectroscopy, vol.59, issue.2, pp.206-226, 2005. ,
DOI : 10.1366/0003702053085007
Chapter 8 Ultrafast Fluorescence Spectroscopy via Upconversion, Methods Enzymol, vol.450, pp.159-183, 2008. ,
DOI : 10.1016/S0076-6879(08)03408-3
Molecular Fluorescence: Principles and Applications, 2009. ,
DOI : 10.1002/9783527650002
Thymine, thymidine and thymidine 5???-monophosphate studied by femtosecond fluorescence upconversion spectroscopy, Chemical Physics Letters, vol.351, issue.3-4, pp.3-4195, 2002. ,
DOI : 10.1016/S0009-2614(01)01375-6
URL : https://hal.archives-ouvertes.fr/hal-00144420
Femtosecond fluorescence upconversion setup with broadband detection in the ultraviolet, Optics Letters, vol.32, issue.24, pp.3555-3557, 2007. ,
DOI : 10.1364/OL.32.003555
Femtosecond broadband fluorescence upconversion spectroscopy: Improved setup and photometric correction, Review of Scientific Instruments, vol.82, issue.6, p.63108, 2011. ,
DOI : 10.1063/1.3597674
URL : http://nbn-resolving.de/urn/resolver.pl?urn=urn:nbn:de:bvb:12-bsb00086972-4
Broad-band fluorescence upconversion for femtosecond spectroscopy, Applied Physics Letters, vol.79, issue.5, pp.566-568, 2001. ,
DOI : 10.1063/1.1387257
Subpicosecond kerr-gate spectrofluorometry. From Fluorescence Spectroscopy and Microscopy: Methods and Protocols ,
DOI : 10.1007/978-1-62703-649-8_13
URL : https://hal.archives-ouvertes.fr/hal-00945223
Imaging protein molecules using FRET and FLIM microscopy, Current Opinion in Biotechnology, vol.16, issue.1, pp.19-27, 2005. ,
DOI : 10.1016/j.copbio.2004.12.002
Fluorescent imaging in living systems, Current Opinion in Pharmacology, vol.1, issue.5, pp.521-526, 2001. ,
DOI : 10.1016/S1471-4892(01)00090-X
Characterization of variants altered at the N-terminal proline, a novel heme-axial ligand in CooA, the CO-sensing transcriptional activator, J. Biol. Chem, vol.275, issue.50, pp.39332-39340, 2000. ,
Structure and Mechanism in Protein Science. A guide to Enzyme Catalysis and Protein Folding, Freeman and Company, 1999. ,
Crystal Structure of CO-sensing Transcription Activator CooA Bound to Exogenous Ligand Imidazole, Journal of Molecular Biology, vol.367, issue.3 ,
DOI : 10.1016/j.jmb.2007.01.043
Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: DNA binding specificity based on energetics of DNA kinking, Journal of Molecular Biology, vol.314, issue.1 ,
DOI : 10.1006/jmbi.2001.5089
Structural order of lipids and proteins in membranes: evaluation of fluorescence anisotropy data., Proc. Natl. Acad. Sci, pp.6361-6366, 1979. ,
DOI : 10.1073/pnas.76.12.6361
Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction., Proc. Natl. Acad. Sci, pp.1744-1752, 1990. ,
DOI : 10.1073/pnas.87.5.1744
Probing the physical basis for trp repressor-operator recognition, Journal of Molecular Biology, vol.287, issue.3, pp.539-54, 1999. ,
DOI : 10.1006/jmbi.1999.2625
Enzymes. A practical Introduction to Structure, Mechanism, and Data Analysis, 2000. ,
The transcription factor DNR from Pseudomonas aeruginosa specifically requires nitric oxide and haem for the activation of a target promoter in Escherichia coli, Microbiology, vol.155, issue.9, pp.2838-2882, 2009. ,
DOI : 10.1099/mic.0.028027-0
Probing the Interaction Between Fluorophores and DNA Nucleotides by Fluorescence Correlation Spectroscopy and Fluorescence Quenching???, Photochemistry and Photobiology, vol.85, issue.4 ,
DOI : 10.1111/j.1751-1097.2012.01121.x
Dynamique conformationnelle des protéinesprotéinesétudiée par dichro¨?smedichro¨?sme circulaire résolu en temps, 2013. ,
Dynamique conformationelle de la myoglobine suivie par dichro¨?smedichro¨?sme circulaire résolu temporellement, 2005. ,
How to study proteins by circular dichroism, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1751, issue.2, pp.1751119-139, 2005. ,
DOI : 10.1016/j.bbapap.2005.06.005
Circular Dichroism & Linear Dichroism, 2008. ,
Glotaran: a Java-based Graphical User Interface for the R-package TIMP, J. Stat. Software, issue.3, pp.491-513, 2012. ,
URL : https://hal.archives-ouvertes.fr/hal-00817159
Effect of DNA Binding on Geminate CO Recombination Kinetics in CO-sensing Transcription Factor CooA, Journal of Biological Chemistry, vol.287, issue.26, 2012. ,
DOI : 10.1074/jbc.M112.345090
Dynamics of Carbon Monoxide Binding to CooA, Journal of Biological Chemistry, vol.279, issue.20, pp.27921096-108, 2004. ,
DOI : 10.1074/jbc.M400613200
Geminate recombination of carbon monoxide to myoglobin, Journal of Molecular Biology, vol.166, issue.3, pp.443-451, 1983. ,
DOI : 10.1016/S0022-2836(83)80094-1
Binding of CO at the Pro2 Side Is Crucial for the Activation of CO-sensing Transcriptional Activator CooA. 1H NMR SPECTROSCOPIC STUDIES, Journal of Biological Chemistry, vol.276, issue.15 ,
DOI : 10.1074/jbc.C100047200
Temperature-Dependent Studies of NO Recombination to Heme and Heme Proteins, Journal of the American Chemical Society, vol.127, issue.48, pp.16921-16934, 2005. ,
DOI : 10.1021/ja054249y
Control of Nitric Oxide Dynamics by Guanylate Cyclase in Its Activated State, Journal of Biological Chemistry, vol.276, issue.50, pp.46815-46821, 2001. ,
DOI : 10.1074/jbc.M102224200
URL : https://hal.archives-ouvertes.fr/hal-00837035
Protein fluctuations, distributed coupling, and the binding of ligands to heme proteins, Journal of the American Chemical Society, vol.110, issue.20, pp.6656-6670, 1988. ,
DOI : 10.1021/ja00228a009
A GAF Domain in the Hypoxia/NO-inducible Mycobacterium tuberculosis DosS Protein Binds Haem, Journal of Molecular Biology, vol.353, issue.5, pp.929-936, 2005. ,
DOI : 10.1016/j.jmb.2005.09.011
Ligand Dynamics in an Electron Transfer Protein: PICOSECOND GEMINATE RECOMBINATION OF CARBON MONOXIDE TO HEME IN MUTANT FORMS OF CYTOCHROME c, Journal of Biological Chemistry, vol.282, issue.3, pp.1638-1687, 2007. ,
DOI : 10.1074/jbc.M605760200
URL : https://hal.archives-ouvertes.fr/hal-00097190
Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives, Biophysical Chemistry, vol.98, issue.1-2, pp.65-77, 2002. ,
DOI : 10.1016/S0301-4622(02)00085-6
Photochemical electron injection into redox-active proteins, Proc. Natl. Acad. Sci, pp.6176-6179, 1997. ,
DOI : 10.1073/pnas.94.12.6176
Geminate carbon monoxide rebinding to a c-type haem, Dalton Transactions, vol.279, issue.21, pp.3489-3494, 2005. ,
DOI : 10.1039/b508183c
URL : https://hal.archives-ouvertes.fr/hal-00829233
High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c, Journal of Molecular Biology, vol.214, issue.2 ,
DOI : 10.1016/0022-2836(90)90197-T
Oxygen Signal Transduction, IUBMB Life (International Union of Biochemistry and Molecular Biology: Life), vol.51, issue.3, pp.165-173, 2001. ,
DOI : 10.1080/152165401753544232
Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by wholecell assays suitable for high-throughput screening of biofilm inhibitors ,
Cyclic di-GMP as a bacterial second messenger ,
Common dynamics of globin family proteins, IUBMB Life, vol.59, issue.8, pp.528-534, 2007. ,
DOI : 10.1080/15216540701222914
Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors, Proc. Natl. Acad. Sci, pp.9912771-9912777, 2002. ,
DOI : 10.1073/pnas.192311699
URL : https://hal.archives-ouvertes.fr/hal-00845092
Vibrational Relaxation of the CO Stretch Vibration in Hemoglobin-CO, Myoglobin-CO, and Protoheme-CO, The Journal of Physical Chemistry, vol.99, issue.13, pp.994842-4846, 1995. ,
DOI : 10.1021/j100013a064
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control, Nature, vol.380, issue.6571, pp.380221-226, 1996. ,
DOI : 10.1038/380221a0
Nitric Oxide, Clin. Exp. Pharmacol. Physiol, vol.22, issue.4, pp.305-308, 1995. ,
DOI : 10.1016/B0-12-226870-9/01222-3
Photoexcitation Dynamics of NO-Bound Ferric Myoglobin Investigated by Femtosecond Vibrational Spectroscopy, The Journal of Physical Chemistry B, vol.117, issue.10 ,
DOI : 10.1021/jp400055d
Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase, The EMBO Journal, vol.19, issue.21 ,
DOI : 10.1093/emboj/19.21.5661
Ligand binding and protein relaxation in heme proteins: a room temperature analysis of nitric oxide geminate recombination, Biochemistry, vol.30, issue.16, pp.303975-87, 1991. ,
DOI : 10.1021/bi00230a025
Dynamics of Geminate Recombination of NO with Myoglobin in Aqueous Solution Probed by Femtosecond Mid-IR Spectroscopy, The Journal of Physical Chemistry B, vol.108, issue.52 ,
DOI : 10.1021/jp0489020
Nitrosyliron(III) Porphyrinates:?? Porphyrin Core Conformation and FeNO Geometry. Any Correlation?, Journal of the American Chemical Society, vol.124, issue.46 ,
DOI : 10.1021/ja0207145
XL1-Blue competent cells, Stratagene, An Agilent Technologies division, 2011. ,
Experiments in Molecular Genetics, 1972. ,
An Enhanced System for Unnatural Amino Acid Mutagenesis in E. coli, Journal of Molecular Biology, vol.395, issue.2, pp.361-74, 2010. ,
DOI : 10.1016/j.jmb.2009.10.030
Molecular Cloning. A Laboratory Manual, 1989. ,
Modern Optical Spectroscopy. With Exercises and Examples from Biophysics and Biochemistry, 2009. ,
CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein, Proceedings of the National Academy of Sciences, vol.94, issue.21 ,
DOI : 10.1073/pnas.94.21.11216
Measurement of protein using bicinchoninic acid, Analytical Biochemistry, vol.150, issue.1, pp.76-85, 1985. ,
DOI : 10.1016/0003-2697(85)90442-7
Negative dispersion using pairs of prisms, Optics Letters, vol.9, issue.5, pp.150-152, 1984. ,
DOI : 10.1364/OL.9.000150
Azide-Alkyne Coupling: A Powerful Reaction for Bioconjugate Chemistry, ChemBioChem, vol.7, issue.11, 2003. ,
DOI : 10.1002/cbic.200300705
Addition of p-azido-l-phenylalanine to the genetic code of Escherichia coli, J ,
The Reaction of Reduced Xanthine Dehydrogenase with Molecular Oxygen: REACTION KINETICS AND MEASUREMENT OF SUPEROXIDE RADICAL, Journal of Biological Chemistry, vol.272, issue.13 ,
DOI : 10.1074/jbc.272.13.8370
optical Kerr gate, Applied Physics Letters, vol.26, issue.3, pp.92-93, 1975. ,
DOI : 10.1063/1.88092
Highly efficient ultrafast optical Kerr shutters with the use of organic nonlinear materials, Journal of the Optical Society of America B, vol.11, issue.11, pp.2216-2223, 1994. ,
DOI : 10.1364/JOSAB.11.002216
Hemoglobin and Myoglobin in their Reactions with Ligands. North Holland -American, 1971. ,