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Am. Chem. Soc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib117","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1366\/0003702011951696","article-title":"Time-resolved FT-IR spectroscopy of chemical reactions in solution by fast diffusion-based mixing in a micromachined flow cell","volume":"55","author":"Hinsmann","year":"2001","journal-title":"Appl. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib118","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1042\/bj3060843","article-title":"A stopped-flow apparatus for infrared spectroscopy of aqueous solutions","volume":"306","author":"White","year":"1995","journal-title":"Biochem. 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Univ.\u2014Chinese"},{"key":"10.1016\/j.bbabio.2007.06.004_bib167","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1366\/0003702944028065","article-title":"Secondary structure estimation of proteins using the amide-III region of Fourier-transform infrared-spectroscopy\u2014Application to analyze calcium binding-induced structural-changes in calsequestrin","volume":"48","author":"Fu","year":"1994","journal-title":"Appl. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib168","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0301-4622(99)00060-5","article-title":"Identification of \u00df-turn and random coil amide III infrared bands for secondary structure estimation of proteins","volume":"80","author":"Cai","year":"1999","journal-title":"Biophys. 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A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib254","doi-asserted-by":"crossref","first-page":"6114","DOI":"10.1073\/pnas.95.11.6114","article-title":"Fourier transform infrared spectroscopy reveals a rigid \u03b1-helical assembly for the tetrameric Streptomyces lividans K+ channel","volume":"95","author":"Le Coutre","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib255","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1016\/S0021-9258(17)35695-8","article-title":"Infrared spectroscopic study of photoreceptor membrane and purple membrane","volume":"261","author":"Downer","year":"1986","journal-title":"J. Biol. 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Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib266","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1021\/bi00544a012","article-title":"Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy","volume":"19","author":"Belasco","year":"1980","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib267","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1042\/bj2580599","article-title":"Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids","volume":"258","author":"Tonge","year":"1989","journal-title":"Biochem. 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Mol. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib293","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1063\/1.460303","article-title":"Spectra of dangling OH groups at ice cluster surfaces and within pores of amorphous ice","volume":"94","author":"Rowland","year":"1991","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbabio.2007.06.004_bib294","doi-asserted-by":"crossref","first-page":"085401","DOI":"10.1103\/PhysRevB.66.085401","article-title":"Sum-frequency spectroscopic studies of ice interfaces","volume":"66","author":"Wei","year":"2002","journal-title":"Phys. Rev., B"},{"key":"10.1016\/j.bbabio.2007.06.004_bib295","doi-asserted-by":"crossref","first-page":"3005","DOI":"10.1039\/b506641g","article-title":"The effect of cooperative hydrogen bonding on the OH stretching-band shift for water clusters studied by matrix-isolation infrared spectroscopy and density functional theory","volume":"7","author":"Ohno","year":"2005","journal-title":"Phys. Chem. Chem. 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Phys."},{"key":"10.1016\/j.bbabio.2007.06.004_bib299","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1126\/science.1081634","article-title":"Gas-phase infrared spectrum of the protonated water dimer","volume":"299","author":"Asmis","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.bbabio.2007.06.004_bib300","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1139\/v57-160","article-title":"Infrared spectrum of the H3O+ ion in aqueous solutions","volume":"35","author":"Falk","year":"1957","journal-title":"Can. J. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib301","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/0301-0104(79)80155-X","article-title":"H+ and OH\u2212 ions in aqueous solutions. Vibrational spectra of hydrates","volume":"39","author":"Librovich","year":"1979","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bbabio.2007.06.004_bib302","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1023\/A:1005972514425","article-title":"Proton uptake upon quinone reduction in bacterial reaction centers: IR signature and possible participation of a highly polarizable hydrogen bond network","volume":"55","author":"Breton","year":"1998","journal-title":"Photosynth. Res."},{"key":"10.1016\/j.bbabio.2007.06.004_bib303","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1063\/1.1423327","article-title":"The vibrational spectrum of the hydrated proton: Comparison of experiment, simulation, and normal mode analysis","volume":"116","author":"Kim","year":"2002","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbabio.2007.06.004_bib304","doi-asserted-by":"crossref","first-page":"6635","DOI":"10.1021\/bi9600456","article-title":"D38 is an essential part of the proton translocation pathway in bacteriorhodopsin","volume":"35","author":"Riesle","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib305","doi-asserted-by":"crossref","first-page":"5001","DOI":"10.1021\/bi971701k","article-title":"Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network","volume":"37","author":"Rammelsberg","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib306","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0006-3495(01)76075-4","article-title":"Time-resolved Fourier transform infrared spectroscopy of the polarizable proton continua and the proton pump mechanism of bacteriorhodopsin","volume":"80","author":"Wang","year":"2001","journal-title":"Biophys. 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Ed."},{"key":"10.1016\/j.bbabio.2007.06.004_bib309","doi-asserted-by":"crossref","first-page":"5448","DOI":"10.1021\/bi00071a022","article-title":"Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: evidence for specific protein structural changes upon desensitization","volume":"32","author":"Baenziger","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib310","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1016\/S0006-3495(92)81905-7","article-title":"Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy","volume":"61","author":"Baenziger","year":"1992","journal-title":"Biophys. 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Biophys. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib314","first-page":"243","article-title":"Caged nucleotides and neurotransmitters","volume":"Vol. 2","author":"Corrie","year":"1993"},{"key":"10.1016\/j.bbabio.2007.06.004_bib315","series-title":"Optical Methods in Cell Physiology","first-page":"417","article-title":"Design and application of photolabile intracellular probes","author":"Nerbonne","year":"1986"},{"key":"10.1016\/j.bbabio.2007.06.004_bib316","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1146\/annurev.bb.11.060182.001055","article-title":"Physiological and pharmacological manipulations with light flashes","volume":"11","author":"Lester","year":"1982","journal-title":"Annu. Rev. Biophys. 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A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle","volume":"277","author":"Barth","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbabio.2007.06.004_bib319","doi-asserted-by":"crossref","first-page":"10311","DOI":"10.1021\/ja00146a015","article-title":"Photochemical release of ATP from \u2018caged ATP\u2019 studied by time-resolved infrared spectroscopy","volume":"117","author":"Barth","year":"1995","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib320","doi-asserted-by":"crossref","first-page":"4149","DOI":"10.1021\/ja964430u","article-title":"Time-resolved infrared spectroscopy of intermediates and products from photolysis of 1-(2-nitrophenyl)ethyl phosphates: reaction of the 2-nitrosoacetophenone byproduct with thiols","volume":"119","author":"Barth","year":"1997","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib321","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0076-6879(98)91015-1","article-title":"Fourier transform infrared photolysis studies of caged compounds","volume":"291","author":"Cepus","year":"1998","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib322","series-title":"Dynamic Studies in Biology: Phototriggers, Photoswitches and Caged Biomolecules","article-title":"Time-resolved IR spectroscopy with caged compounds: An introduction","author":"Barth","year":"2005"},{"key":"10.1016\/j.bbabio.2007.06.004_bib323","doi-asserted-by":"crossref","first-page":"3615","DOI":"10.1529\/biophysj.104.055368","article-title":"Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase","volume":"88","author":"Liu","year":"2005","journal-title":"Biophys. 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Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib327","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.chemphys.2005.08.033","article-title":"Fast folding dynamics of \u03b1-helical peptides \u2014 Effect of solvent additives and pH","volume":"323","author":"Ramajo","year":"2006","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bbabio.2007.06.004_bib328","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1006\/jmbi.1997.1454","article-title":"Structural characterization of the pressure-denatured state and unfolding\/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy","volume":"275","author":"Panick","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib329","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.1021\/bi992176n","article-title":"Pressure-induced unfolding\/refolding of ribonuclease A: static and kinetic Fourier transform infrared spectroscopy study","volume":"39","author":"Panick","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib330","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1111\/j.1432-1033.1990.tb15338.x","article-title":"Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c","volume":"187","author":"Moss","year":"1990","journal-title":"Eur. J. 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A flash photolysis study of flavin photoreduction by ethylenediaminetetraacetate and nitrilotriacetate","volume":"21","author":"Traber","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib343","doi-asserted-by":"crossref","first-page":"16253","DOI":"10.1021\/bi991759u","article-title":"Changes in secondary structure and salt links of cytochrome P-450cam induced by photoreduction: A Fourier transform infrared spectroscopic study","volume":"38","author":"Contzen","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib344","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/S0014-5793(96)01174-X","article-title":"Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases","volume":"397","author":"L\u00fcbben","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbabio.2007.06.004_bib345","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1021\/bi981859k","article-title":"Electron transfer induces side-chain conformational changes of glutamate-286 from cytochrome bo3","volume":"38","author":"L\u00fcbben","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib346","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1093\/oxfordjournals.jbchem.a022423","article-title":"Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy","volume":"126","author":"Yamazaki","year":"1999","journal-title":"J. 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The enzyme at work","volume":"271","author":"Barth","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib350","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/85021","article-title":"Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy","volume":"8","author":"Brudler","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib351","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1042\/bj3380153","article-title":"Hydrogen bonding and protein perturbation in \u00df-lactam acyl-enzymes of streptococcus pneumoniae penicilin-binding protein PBP2x","volume":"338","author":"Chittock","year":"1999","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib352","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1016\/S0006-3495(96)79537-1","article-title":"A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca2+-ATPase: kinetics of the high-affinity calcium binding at low temperature","volume":"71","author":"Troullier","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib353","doi-asserted-by":"crossref","first-page":"49902","DOI":"10.1074\/jbc.M408062200","article-title":"Phosphorylation of the sarcoplasmic reticulum Ca2+-ATPase from ATP and ATP analogs studied by infrared spectroscopy","volume":"279","author":"Liu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib354","first-page":"401","article-title":"Chlorophyll aggregation: coordination interactions in chlorophyll monomers, dimers, and oligomers","volume":"vol. 5","author":"Katz","year":"1978"},{"key":"10.1016\/j.bbabio.2007.06.004_bib355","series-title":"The Chlorophylls","first-page":"185","article-title":"Infrared and nuclear magnetic resonance spectroscopy of chlorophyll","author":"Katz","year":"1966"},{"key":"10.1016\/j.bbabio.2007.06.004_bib356","series-title":"Chlorophylls","first-page":"855","article-title":"Vibrational spectroscopy of chlorophylls","author":"Lutz","year":"1991"},{"key":"10.1016\/j.bbabio.2007.06.004_bib357","doi-asserted-by":"crossref","first-page":"4699","DOI":"10.1021\/bi00389a016","article-title":"Oxygen infrared spectra of oxyhemoglobins and oxymyoglobins. Evidence of two major liganded O2 structures","volume":"26","author":"Potter","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib358","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1042\/bj2880167","article-title":"The binding of amide substrate analogues to phospholipase A2","volume":"288","author":"Slaich","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib359","doi-asserted-by":"crossref","first-page":"8492","DOI":"10.1074\/jbc.275.12.8492","article-title":"The mechanism of GTP hydrolysis by ras probed by Fourier transform infrared spectroscopy","volume":"275","author":"Du","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib360","doi-asserted-by":"crossref","first-page":"3037","DOI":"10.1021\/bi0017024","article-title":"Ras catalyzes GTP hydrolysis by shifting negative charges from \u03b3- to \u00df-phosphate as revealed by time-resolved FTIR difference spectroscopy","volume":"40","author":"Allin","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib361","doi-asserted-by":"crossref","first-page":"4352","DOI":"10.1529\/biophysj.105.061689","article-title":"Interactions of phosphate groups of ATP and aspartyl phosphate with the sarcoplasmic reticulum Ca2+-ATPase. An FTIR study","volume":"89","author":"Liu","year":"2005","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib362","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1002\/j.1460-2075.1986.tb04285.x","article-title":"Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labeled retinals","volume":"5","author":"Gerwert","year":"1986","journal-title":"EMBO J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib363","doi-asserted-by":"crossref","first-page":"6279","DOI":"10.1021\/bi00142a016","article-title":"Potential of 13C and 15N labeling for studying protein\u2013protein interactions using Fourier transform infrared spectroscopy","volume":"31","author":"Haris","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib364","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/nsb0894-512","article-title":"Site-directed isotope labeling and FTIR spectroscopy of bacteriorhodopsin","volume":"1","author":"Sonar","year":"1994","journal-title":"Struct. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib365","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/nsb0894-495","article-title":"New tool for spectroscopists","volume":"1","author":"Spudich","year":"1994","journal-title":"Struct. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib366","series-title":"Infrared Spectroscopy of Biomolecules","first-page":"341","article-title":"New trends in isotope-edited infrared spectroscopy","author":"Fabian","year":"1996"},{"key":"10.1016\/j.bbabio.2007.06.004_bib367","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1021\/ar050135f","article-title":"Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy","volume":"39","author":"Decatur","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbabio.2007.06.004_bib368","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/j.cbpa.2006.08.013","article-title":"Isotope-edited IR spectroscopy for the study of membrane proteins","volume":"10","author":"Arkin","year":"2006","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib369","doi-asserted-by":"crossref","first-page":"33209","DOI":"10.1074\/jbc.274.47.33209","article-title":"Insight into the secondary structure of non-native proteins bound to a molecular chaperone \u03b1-crystallin\u2014An isotope-edited infrared spectroscopic study","volume":"274","author":"Das","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib370","doi-asserted-by":"crossref","first-page":"10883","DOI":"10.1021\/bi00202a006","article-title":"Isotope-edited Fourier transform infrared spectroscopy studies of calmodulin's interaction with its target peptides","volume":"33","author":"Zhang","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib371","doi-asserted-by":"crossref","first-page":"1728","DOI":"10.1016\/S0006-3495(96)79735-7","article-title":"Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban","volume":"70","author":"Ludlam","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib372","doi-asserted-by":"crossref","first-page":"11914","DOI":"10.1021\/ja991279q","article-title":"Isotope-edited infrared spectroscopy of helical peptides","volume":"121","author":"Decatur","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib373","doi-asserted-by":"crossref","first-page":"8318","DOI":"10.1073\/pnas.140161997","article-title":"Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution","volume":"97","author":"Silva","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib374","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1034\/j.1399-3011.2000.00693.x","article-title":"Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy","volume":"55","author":"Gordon","year":"2000","journal-title":"J. Peptide Res."},{"key":"10.1016\/j.bbabio.2007.06.004_bib375","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1038\/nsb1195-990","article-title":"Structural model for the \u00df-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide","volume":"2","author":"Lansbury","year":"1995","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib376","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/0006-291X(81)90478-2","article-title":"Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy","volume":"103","author":"Rothschild","year":"1981","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbabio.2007.06.004_bib377","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/0076-6879(82)88090-7","article-title":"Kinetic properties of rhodopsin and bacteriorhodopsin measured by kinetic infrared spectroscopy (KIS)","volume":"88","author":"M\u00e4ntele","year":"1982","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib378","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/0014-5793(82)80021-5","article-title":"Evidence for the protonation of two internal carboxylic groups during the photocycle of bacteriorhodopsin","volume":"141","author":"Siebert","year":"1982","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbabio.2007.06.004_bib379","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1021\/bi00054a018","article-title":"Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin","volume":"32","author":"Sasaki","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib380","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1073\/pnas.88.6.2388","article-title":"Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates","volume":"88","author":"Braiman","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib381","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1016\/S0006-3495(92)81722-8","article-title":"Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy","volume":"63","author":"Souvignier","year":"1992","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib382","doi-asserted-by":"crossref","first-page":"1394","DOI":"10.1366\/0003702934067351","article-title":"Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: identification of chromophore twists by bending vibrations","volume":"47","author":"Weidlich","year":"1993","journal-title":"Appl. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib383","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1366\/0003702971940585","article-title":"Molecular reaction mechanisms of proteins monitored by nanosecond step-scan FT-IR difference spectroscopy","volume":"51","author":"Rammelsberg","year":"1997","journal-title":"Appl. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib384","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1021\/bi00323a024","article-title":"Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane","volume":"24","author":"Engelhard","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib385","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1111\/j.1751-1097.1992.tb09731.x","article-title":"Identification of the proton acceptor of Schiff-base deprotonation in bacteriorhodopsin \u2014 a Fourier-transform-infrared study of the mutant Asp85\u2192Glu in its natural lipid environment","volume":"56","author":"Fahmy","year":"1992","journal-title":"Photochem. Photobiol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib386","doi-asserted-by":"crossref","first-page":"4684","DOI":"10.1021\/bi00134a022","article-title":"Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy","volume":"31","author":"Maeda","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib387","doi-asserted-by":"crossref","first-page":"8516","DOI":"10.1021\/bi00423a002","article-title":"Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212","volume":"27","author":"Braiman","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib388","doi-asserted-by":"crossref","first-page":"4943","DOI":"10.1073\/pnas.86.13.4943","article-title":"Role of aspartate-96 in proton translocation by bacteriorhodopsin","volume":"86","author":"Gerwert","year":"1989","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib389","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/35020654","article-title":"Bacteriorhodopsin\u2014The movie","volume":"406","author":"K\u00fchlbrandt","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.bbabio.2007.06.004_bib390","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1016\/j.jmb.2006.11.016","article-title":"Structural changes in the L photointermediate of bacteriorhodopsin","volume":"365","author":"Lanyi","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib391","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1111\/j.1432-1033.1983.tb07187.x","article-title":"Investigation of the primary photochemistry of bacteriorhodopsin by low-temperature Fourier-transform infrared spectroscopy","volume":"130","author":"Siebert","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib392","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0022-2860(89)80017-1","article-title":"Photoisomerization in bacteriorhodopsin studied by FTIR linear dichroism and photoselection experiments combined with quantum chemical theoretical analysis","volume":"214","author":"Fahmy","year":"1989","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bbabio.2007.06.004_bib393","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/S0006-3495(91)82136-1","article-title":"Structural investigation of bacteriorhodopsin and some of its photoproducts by polarized Fourier transform infrared spectroscopic methods \u2014 difference spectroscopy and photoselection","volume":"60","author":"Fahmy","year":"1991","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib394","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.jmb.2007.02.021","article-title":"Inter-helical hydrogen bonds are essential elements for intra-protein signal transduction: the role of Asp115 in bacteriorhodopsin transport function","volume":"368","author":"Per\u00e1lvarez-Mar\u00edn","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbabio.2007.06.004_bib395","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0022-2860(94)87019-5","article-title":"Hydrogen-bonded chains with large proton polarizability as charge conductors in proteins bacteriorhodopsin and the F0 subunit of E. coli","volume":"322","author":"Zundel","year":"1994","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bbabio.2007.06.004_bib396","doi-asserted-by":"crossref","first-page":"9774","DOI":"10.1073\/pnas.87.24.9774","article-title":"Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy","volume":"87","author":"Gerwert","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib397","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/S0006-3495(96)79637-6","article-title":"A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins","volume":"70","author":"Braiman","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib398","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.1021\/bi00059a015","article-title":"Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformation change","volume":"32","author":"Cao","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib399","doi-asserted-by":"crossref","first-page":"1706","DOI":"10.1016\/S0006-3495(94)80644-7","article-title":"pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy","volume":"67","author":"Sz\u00e1raz","year":"1994","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib400","doi-asserted-by":"crossref","first-page":"10070","DOI":"10.1021\/bi990873+","article-title":"Fourier transform infrared spectra of the late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212","volume":"38","author":"Dioumaev","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib401","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1006\/bbrc.2001.4730","article-title":"Time-resolved FT-IR spectroscopic investigation of the pH-dependent proton transfer reactions in the E194Q mutant of bacteriorhodopsin","volume":"283","author":"Zscherp","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbabio.2007.06.004_bib402","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1073\/pnas.78.1.234","article-title":"Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex","volume":"78","author":"Alben","year":"1981","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib403","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0014-5793(01)02769-7","article-title":"Perfusion-induced redox differences in cytochrome c oxidase: ATR\/FT-IR spectroscopy","volume":"505","author":"Nyquist","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbabio.2007.06.004_bib404","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1021\/bi0109717","article-title":"Attenuated total reflection Fourier transform infrared studies of redox change in bovine cytochrome c oxidase: resolution of the redox Fourier transform infrared difference spectrum of heme a3","volume":"41","author":"Rich","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib405","doi-asserted-by":"crossref","first-page":"10905","DOI":"10.1021\/bi00091a046","article-title":"Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides","volume":"32","author":"Calhoun","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib406","doi-asserted-by":"crossref","first-page":"8715","DOI":"10.1073\/pnas.1530408100","article-title":"Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase","volume":"100","author":"Nyquist","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib407","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1126\/science.280.5370.1723","article-title":"Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase","volume":"280","author":"Yoshikawa","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.bbabio.2007.06.004_bib408","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1021\/bi002154x","article-title":"Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coli","volume":"40","author":"Hellwig","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib409","doi-asserted-by":"crossref","first-page":"9116","DOI":"10.1021\/bi012056r","article-title":"Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes","volume":"41","author":"Hellwig","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib410","doi-asserted-by":"crossref","first-page":"14383","DOI":"10.1021\/bi026370c","article-title":"Direct infrared detection of the covalently ring linked His\u2013Tyr structure in the active site of the heme-copper oxidases","volume":"41","author":"Tomson","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib411","doi-asserted-by":"crossref","first-page":"10873","DOI":"10.1021\/bi061114b","article-title":"Structural and chemical changes of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidine","volume":"45","author":"Iwaki","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib412","doi-asserted-by":"crossref","first-page":"14370","DOI":"10.1021\/bi048545j","article-title":"ATR-FTIR spectroscopy and isotope labeling of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase","volume":"43","author":"Iwaki","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib413","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/0005-2736(92)90152-C","article-title":"The effect of dicyclohexylcarbodiimide and cyclopiazonic acid on the difference FTIR spectra of sarcoplasmic reticulum induced by photolysis of caged-ATP and caged-Ca2+","volume":"1104","author":"Buchet","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbabio.2007.06.004_bib414","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0005-2736(91)90126-S","article-title":"Ca2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum","volume":"1069","author":"Buchet","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbabio.2007.06.004_bib415","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0005-2728(94)90032-9","article-title":"Structural changes of sarcoplasmic reticulum Ca2+ ATPase upon Ca2+ binding studied by simultaneous measurement of infrared absorbance changes and changes of intrinsic protein fluorescence","volume":"1188","author":"Georg","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbabio.2007.06.004_bib416","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1002\/bip.10113","article-title":"Mapping nucleotide binding site of calcium ATPase with IR spectroscopy: effects of ATP \u03b3-phosphate binding","volume":"67","author":"Liu","year":"2002","journal-title":"Biopolymers (Biospectroscopy)"},{"key":"10.1016\/j.bbabio.2007.06.004_bib417","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/nature02680","article-title":"Crystal structure of the calcium pump with a bound ATP analogue","volume":"430","author":"Toyoshima","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.bbabio.2007.06.004_bib418","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1126\/science.1099366","article-title":"Phosphoryl transfer and calcium ion occlusion in the calcium pump","volume":"304","author":"S\u00f8rensen","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.bbabio.2007.06.004_bib419","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1016\/S0021-9258(19)44022-2","article-title":"Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles","volume":"248","author":"Kanazawa","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbabio.2007.06.004_bib420","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/bip.10085","article-title":"Selective monitoring of 3 out of 50,000 protein vibrations","volume":"67","author":"Barth","year":"2002","journal-title":"Biopolymers (Biospectroscopy)"},{"key":"10.1016\/j.bbabio.2007.06.004_bib421","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1107\/S0108768192002453","article-title":"Chemical and steric constraints in inorganic solids","volume":"B48","author":"Brown","year":"1992","journal-title":"Acta Cryst."},{"key":"10.1016\/j.bbabio.2007.06.004_bib422","doi-asserted-by":"crossref","first-page":"5862","DOI":"10.1021\/bi00073a020","article-title":"Aspartic acid-212 of bacteriorhodopsin is ionized in the M and N photocycle intermediates: an FTIR study on specifically 13C-labeled reconstituted purple membranes","volume":"32","author":"Fahmy","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib423","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.1021\/bi00059a015","article-title":"Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein conformational change","volume":"32","author":"Cao","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib424","doi-asserted-by":"crossref","first-page":"4744","DOI":"10.1021\/jp983011b","article-title":"Modeling vibrational spectra of amino acid side chains in proteins: effects of protonation state, counterion, and solvent on arginine CN stretch frequencies","volume":"103","author":"Braiman","year":"1999","journal-title":"J. Phys. Chem., B"},{"key":"10.1016\/j.bbabio.2007.06.004_bib425","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1002\/j.1460-2075.1995.tb07148.x","article-title":"Chemical reconstitution of a chloride pump inactivated by a single point mutation","volume":"14","author":"Rudiger","year":"1995","journal-title":"EMBO J."},{"key":"10.1016\/j.bbabio.2007.06.004_bib426","doi-asserted-by":"crossref","first-page":"4253","DOI":"10.1021\/jp000157d","article-title":"Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: Infrared and Raman markers of the protonation state of a histidine side chain","volume":"104","author":"Hasegawa","year":"2000","journal-title":"J. Phys. 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Soc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib430","doi-asserted-by":"crossref","first-page":"10725","DOI":"10.1021\/bi00201a021","article-title":"Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy","volume":"33","author":"Fabian","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbabio.2007.06.004_bib431","series-title":"Infrared Spectroscopy of Biomolecules","first-page":"159","article-title":"Fourier transform infrared spectroscopy in the study of hydrated lipids and lipid bilayer membranes","author":"Lewis","year":"1996"},{"key":"10.1016\/j.bbabio.2007.06.004_bib432","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1002\/bip.360240805","article-title":"Vibrational analysis of peptides, polypeptides, and proteins. 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A."},{"key":"10.1016\/j.bbabio.2007.06.004_bib438","series-title":"Infrared Spectra of Labelled Compounds","author":"Pinchas","year":"1971"},{"key":"10.1016\/j.bbabio.2007.06.004_bib439","first-page":"166","article-title":"Etude du spectre de vibration de la dl-serine et des ses d\u00e9riv\u00e9s deuteries","volume":"23","author":"Madec","year":"1978","journal-title":"Can. J. Spectrosc."},{"key":"10.1016\/j.bbabio.2007.06.004_bib440","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/0584-8539(80)80062-6","article-title":"Etude par spectrom\u00e9trie i.r. et Raman de l'indole et de l'indolizine. Liaison hydrog\u00e8ne NH\u22efpi*","volume":"36","author":"Lauti\u00e9","year":"1980","journal-title":"Spectrochim. Acta, A Mol. 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