Water Transport in Proton Exchange Membranes: Insights from Time-Resolved Infrared Spectroscopy

2019 ◽  
Vol 33 (1) ◽  
pp. 1029-1033 ◽  
Author(s):  
Daniel Hallinan ◽  
Maria Grazia De Angelis ◽  
Marco Giacinti Baschetti ◽  
Giulio Sarti ◽  
Yossef A. Elabd
Keyword(s):  
Infrared Spectroscopy ◽  
Water Transport ◽  
Proton Exchange Membranes ◽  
Proton Exchange ◽  
Time Resolved ◽  
Time Resolved Infrared Spectroscopy

A quantum cascade laser setup for studying irreversible photoreactions in H2O with nanosecond resolution and microlitre consumption

2020 ◽  
Vol 22 (45) ◽  
pp. 26459-26467
Author(s):  
Jessica L. Klocke ◽  
Tilman Kottke
Keyword(s):  
Infrared Spectroscopy ◽  
Quantum Cascade Laser ◽  
Time Resolved ◽  
Quantum Cascade ◽  
Time Resolved Infrared Spectroscopy ◽  
Laser Setup

Flavin photoreduction in H2O is elucidated by developing a quantum cascade laser setup for time-resolved infrared spectroscopy on irreversible reactions.

Effect of Annealing Temperature on Back Electron Transfer and Distribution of Deep Trap Sites in Dye-Sensitized TiO2, Studied by Time-Resolved Infrared Spectroscopy

2004 ◽  
Vol 108 (9) ◽  
pp. 2963-2969 ◽  
Author(s):  
Kan Takeshita ◽  
Yutaka Sasaki ◽  
Masahiro Kobashi ◽  
Yuki Tanaka ◽  
Shuichi Maeda ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Infrared Spectroscopy ◽  
Annealing Temperature ◽  
Deep Trap ◽  
Time Resolved ◽  
Dye Sensitized ◽  
Back Electron Transfer ◽  
Time Resolved Infrared Spectroscopy

scholarly journals Probing the Contributions to DNA Hybridization Dynamics with Time-Resolved Infrared Spectroscopy

2021 ◽  
Vol 120 (3) ◽  
pp. 8a-9a
Author(s):  
Brennan Ashwood ◽  
Paul J. Sanstead ◽  
Qing Dai ◽  
Chuan He ◽  
Andrei Tokmakoff
Keyword(s):  
Infrared Spectroscopy ◽  
Dna Hybridization ◽  
Time Resolved ◽  
Time Resolved Infrared Spectroscopy

Photoinduced Energy Transfer in a Conformationally Flexible Re(I)/Ru(II) Dyad Probed by Time-Resolved Infrared Spectroscopy: Effects of Conformation and Spatial Localization of Excited States

2008 ◽  
Vol 47 (12) ◽  
pp. 5071-5078 ◽  
Author(s):  
Timothy L. Easun ◽  
Wassim Z. Alsindi ◽  
Michael Towrie ◽  
Kate L. Ronayne ◽  
Xue-Zhong Sun ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Infrared Spectroscopy ◽  
Excited States ◽  
Spatial Localization ◽  
Time Resolved ◽  
Time Resolved Infrared Spectroscopy

scholarly journals Conformational Changes Generated in GroEL during ATP Hydrolysis as Seen by Time-resolved Infrared Spectroscopy

1999 ◽  
Vol 274 (9) ◽  
pp. 5508-5513 ◽  
Author(s):  
Frithjof von Germar ◽  
Asier Galán ◽  
Oscar Llorca ◽  
Jose L. Carrascosa ◽  
Jose M. Valpuesta ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Conformational Changes ◽  
Atp Hydrolysis ◽  
Time Resolved ◽  
Time Resolved Infrared Spectroscopy

scholarly journals Photochemical Release of ATP from "Caged ATP" Studied by Time-Resolved Infrared Spectroscopy

1995 ◽  
Vol 117 (41) ◽  
pp. 10311-10316 ◽  
Author(s):  
Andreas Barth ◽  
Karin Hauser ◽  
Werner Maentele ◽  
John E. T. Corrie ◽  
David R. Trentham
Keyword(s):  
Infrared Spectroscopy ◽  
Time Resolved ◽  
Caged Atp ◽  
Time Resolved Infrared Spectroscopy

scholarly journals Structural dynamics of the Ca2+-ATPase studied by time-resolved infrared spectroscopy

2008 ◽  
Vol 22 (2-3) ◽  
pp. 63-82 ◽  
Author(s):  
Andreas Barth
Keyword(s):  
Infrared Spectroscopy ◽  
Structural Dynamics ◽  
Ground State ◽  
Transfer Reaction ◽  
High Reactivity ◽  
Acetyl Phosphate ◽  
Time Resolved ◽  
Closed Conformation ◽  
Sarcoplasmic Reticulum Membrane ◽  
Time Resolved Infrared Spectroscopy

This review discusses the contribution of time-resolved infrared spectroscopy to the understanding of the Ca2+pump in the sarcoplasmic reticulum membrane of skeletal muscle cells (SERCA1a). The focus is on interactions of the substrate ATP with the ATPase and on the bond parameters of the phosphoenzyme phosphate group. Functional groups throughout the ATP molecule are important for stabilising the closed conformation of the ATP–ATPase complex and for fast phosphorylation of the ATPase. Dissociation of the reaction product ADP after phosphorylation leads to a more open average conformation of the enzyme and does not trigger the transition from the first phosphoenzyme Ca2E1P to the second E2P. The P–O bond between phosphate and aspartyl moieties is weaker in Ca2E1P and E2P than in acetyl phosphate in aqueous solution, which explains the high reactivity of the phosphoenzymes. This ground state property of the phosphoenzymes prepares for a phosphate transfer reaction with dissociative character.

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