scholarly journals Some Recent Developments in Atomic Lifetime Determinations

1986 ◽  
Vol 39 (5) ◽  
pp. 829 ◽  
Author(s):  
P Hannaford ◽  
RM Lowe
Keyword(s):  
Laser Excitation ◽  
Pulsed Laser ◽  
Fluorescence Decay ◽  
Gas Discharge ◽  
Rare Gas ◽  
Time Resolved ◽  
Atomic Systems ◽  
Refractory Elements ◽  
Wide Range ◽  
Recent Developments

A lifetimes technique that is readily applicable to neutral and singly ionised atoms of a wide range of elements, including the highly refractory elements, is reviewed. With this technique an atomic vapour of the element under study is generated by cathodic sputtering in a low pressure rare-gas discharge and fluorescence decay signals emitted by the vapour following pulsed laser excitation are recorded directly in a fast transient digitiser. Theoretical expressions are presented for the form of the time-resolved fluor~scence signal appropriate to the collisional environment of a rare-gas sputtering discharge. A summary is given of the atomic systems studied to date using this technique, and some new results for Sm and Ba are compared with recently reported results for these elements.

Time-resolved luminescence of CdGaInS4 under pulsed laser excitation at 30 K

1986 ◽  
Vol 133 (1) ◽  
pp. 379-388 ◽  
Author(s):  
M. Colocci ◽  
F. Fermi ◽  
R. Querzoli ◽  
A. Vinattieri
Keyword(s):  
Laser Excitation ◽  
Pulsed Laser ◽  
Time Resolved

Time-resolved emission studies of poly(n-v1nyl carbazole) using pulsed laser excitation

1980 ◽  
Vol 72 (3) ◽  
pp. 554-556 ◽  
Author(s):  
A.J. Roberts ◽  
C.G. Cureton ◽  
D. Phillips
Keyword(s):  
Laser Excitation ◽  
Pulsed Laser ◽  
Time Resolved ◽  
Emission Studies

Triggered infrared spectroscopy for investigating metalloprotein chemistry

2010 ◽  
Vol 368 (1924) ◽  
pp. 3713-3731 ◽  
Author(s):  
Kylie A. Vincent
Keyword(s):  
Ir Spectroscopy ◽  
Cell Metabolism ◽  
Time Resolved ◽  
Technical Developments ◽  
Wide Range ◽  
Gas Atmosphere ◽  
Time Domains ◽  
Recent Developments ◽  
Ir Spectroscopic ◽  
Solute Composition

Recent developments in infrared (IR) spectroscopic time resolution, sensitivity and sample manipulation make this technique a powerful addition to the suite of complementary approaches for the study of time-resolved chemistry at metal centres within proteins. Application of IR spectroscopy to proteins has often targeted the amide bands as probes for gross structural change. This article focuses on the possibilities arising from recent IR technical developments for studies that monitor localized vibrational oscillators in proteins—native or exogenous ligands such as NO, CO, SCN − or CN − , or genetically or chemically introduced probes with IR-active vibrations. These report on the electronic and coordination state of metals, the kinetics, intermediates and reaction pathways of ligand release, hydrogen-bonding interactions between the protein and IR probe, and the electrostatic character of sites in a protein. Metalloprotein reactions can be triggered by light/dark transitions, an electrochemical step, a change in solute composition or equilibration with a new gas atmosphere, and spectra can be obtained over a range of time domains as far as the sub-picosecond level. We can expect to see IR spectroscopy exploited, alongside other spectroscopies, and crystallography, to elucidate reactions of a wide range of metalloprotein chemistry with relevance to cell metabolism, health and energy catalysis.

Sign in / Sign up

Export Citation Format

Share Document