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

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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 is …
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scholarly articleQ13442814

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P819ADS bibcode1990PNAS...87.9774G
P356DOI10.1073/PNAS.87.24.9774
P932PMC publication ID55256
P698PubMed publication ID11607137
P5875ResearchGate publication ID11743705

P2093author name stringGerwert K
Hess B
Souvignier G
P2860cites workBacteriorhodopsin: a light-driven proton pump in Halobacterium HalobiumQ24536703
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyQ27684426
Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membraneQ28241677
Functions of a New Photoreceptor MembraneQ28242305
Role of aspartate-96 in proton translocation by bacteriorhodopsin.Q30369152
Independent photocycles of the spectrally distinct forms of bacteriorhodopsinQ33643795
Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movementQ33846264
Flash spectroscopy of purple membraneQ34259128
Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsinQ34322532
Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycleQ34325389
Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproductQ34333265
On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsinQ37577190
Vibrational spectra of rhodopsin and bacteriorhodopsinQ38771144
Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pumpQ40818021
A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide.Q40820162
Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinalsQ41894307
Branching reactions in the photocycle of bacteriorhodopsinQ44533316
Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanismQ46106715
Pathways of the rise and decay of the M photointermediate(s) of bacteriorhodopsinQ46869060
Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membraneQ59059042
Kinetic model of bacteriorhodopsin photocycle: pathway from M state to bRQ69670799
Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonates during the photocycleQ69837539
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212Q69847863
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 membraneQ70069607
P433issue24
P407language of work or nameEnglishQ1860
P921main subjectinfrared spectroscopyQ70906
spectroscopyQ483666
P304page(s)9774-9778
P577publication date1990-12-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleSimultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy
P478volume87

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