Role of Arginine-82 in Fast Proton Release during the Bacteriorhodopsin Photocycle:  A Time-Resolved FT-IR Study of Purple Membranes Containing15N-Labeled Arginine†

Biochemistry ◽  
2004 ◽  
Vol 43 (40) ◽  
pp. 12809-12818 ◽  
Author(s):  
Yaowu Xiao ◽  
M. Shane Hutson ◽  
Marina Belenky ◽  
Judith Herzfeld ◽  
Mark S. Braiman
2013 ◽  
Vol 117 (24) ◽  
pp. 12661-12678 ◽  
Author(s):  
Kaustava Bhattacharyya ◽  
Alon Danon ◽  
Baiju K.Vijayan ◽  
Kimberly A. Gray ◽  
Peter C. Stair ◽  
...  

Author(s):  
Anastasia Filtschew ◽  
Pablo Beato ◽  
Søren Birk Rasmussen ◽  
Christian Hess

The role of platinum on the room temperature NOx storage mechanism and the NOx desorption behavior of ceria was investigated by combining online FT-IR gas-phase analysis with in situ Raman...


2020 ◽  
Vol 10 (16) ◽  
pp. 5618-5627 ◽  
Author(s):  
Josefine Schnee ◽  
Marco Daturi ◽  
Mohamad El-Roz

QCL-assisted operando FT-IR spectroscopy revealed the role of surface formate species in the photocatalytic oxidation of methanol over TiO2.


1993 ◽  
Vol 47 (9) ◽  
pp. 1382-1385 ◽  
Author(s):  
M. A. Czarnecki ◽  
N. Katayama ◽  
Y. Ozaki ◽  
M. Satoh ◽  
K. Yoshio ◽  
...  

The electric-field-induced reorientation of (S)-4-methylhexyl 4-[4-(decyloxy) phenylethynyl]-2-fluorobenzate in the Sc* phase was investigated by using an asynchronous time-resolved FT-IR technique. The band assignments were made on the basis of the polarized FT-IR spectra and FT-Raman spectrum. The time-resolved study indicates that the reorientation occurs immediately after the electric field is applied. The molecule reorients as a unit; however the rigid core of the molecule seems to be more mobile than the hydrocarbon chains and needs a shorter period of time for the reorientation. The change of orientation is not completely finished in a 500-μs time period. Of particular note is the behavior of the carbonyl band; this band, usually strong in infrared spectra, is very weak in the time-resolved spectra.


1993 ◽  
Vol 47 (9) ◽  
pp. 1394-1400 ◽  
Author(s):  
Olaf Weidlich ◽  
Friedrich Siebert

Sub-microsecond time-resolved step-scan FT-IR spectroscopy is applied to the study of the molecular changes and their dynamics occurring during the KL-L transition of bacteriorhodopsin. The time-resolved difference spectra are compared to the static low-temperature BR → K and BR → L difference spectra. Our data show that the protein part in KL is similar to that in K. However, the chromophore is more relaxed and is differently twisted. A strong hydrogen-out-of-plane (HOOP) mode in KL is assigned to the 15-HOOP. As is the case for L, a strong deformation of the C14-C15 single bond is deduced for KL. Evidence of a KL → L equilibrium is presented. In N, a 15-HOOP mode similar to that in L is observed, indicating very similar twists of the C14-C15 single bond. This observation excludes major contributions of this deformation to the reduction of the pKa of the Schiff base in L. From the spectral changes, important molecular events are deduced that occur in the transitions to KL, L, and N.


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