scholarly journals Time-resolved flow-flash FT-IR difference spectroscopy: the kinetics of CO photodissociation from myoglobin revisited

2009 ◽  
Vol 394 (7) ◽  
pp. 1869-1877 ◽  
Author(s):  
Michael Schleeger ◽  
Christoph Wagner ◽  
Michiel J. Vellekoop ◽  
Bernhard Lendl ◽  
Joachim Heberle
Keyword(s):  
Difference Spectroscopy ◽  
Time Resolved ◽  
Ft Ir ◽  
Kinetics Of

scholarly journals Time-resolved flow-flash FT-IR difference spectroscopy: the kinetics of CO photodissociation from myoglobin revisited

2009 ◽  
Vol 394 (8) ◽  
pp. 2277-2277
Author(s):  
Michael Schleeger ◽  
Christoph Wagner ◽  
Michiel J. Vellekoop ◽  
Bernhard Lendl ◽  
Joachim Heberle
Keyword(s):  
Difference Spectroscopy ◽  
Time Resolved ◽  
Ft Ir ◽  
Kinetics Of

Atr/Ft-Ir Difference Spectroscopy of Biological Matter with Microsecond Time Resolution

1996 ◽  
Vol 50 (5) ◽  
pp. 588-596 ◽  
Author(s):  
Joachim Heberle ◽  
Christian Zscherp
Keyword(s):  
Attenuated Total Reflection ◽  
High Temporal Resolution ◽  
Difference Spectroscopy ◽  
Difference Spectra ◽  
Time Resolved ◽  
Precise Control ◽  
Biological Matter ◽  
Vis Spectroscopy ◽  
Ft Ir ◽  
Atr Spectroscopy

Attenuated total reflection (ATR) spectroscopy allows precise control of external parameters vital for proper functioning of biological matter. For the first time in biospectroscopy, ATR difference spectroscopy has been combined with the step-scan technique. The current setup integrates a broad frequency range (800–25,000 cm−1) with high temporal resolution (5 μs). Vibrations are detected that arise from single amino acids (<10−3 absorbance units) of the chromoprotein bacteriorhodopsin. Time-resolved ATR/FT-IR difference spectra are compared with conventional transmission spectra. The high mirror stability enables time-resolved FT-vis spectroscopy of the same sample with the same instrument. Potential applications even to non-light-absorbing biomaterial are discussed.

Following local light-induced structure changes and dynamics of the photoreceptor PYP with the thiocyanate IR label

2019 ◽  
Vol 21 (12) ◽  
pp. 6622-6634 ◽  
Author(s):  
Larissa Blankenburg ◽  
Lea Schroeder ◽  
Florian Habenstein ◽  
Bartosz Błasiak ◽  
Tilman Kottke ◽  
...  
Keyword(s):  
Steady State ◽  
Ir Spectroscopy ◽  
Local Structure ◽  
Time Resolved ◽  
Structure Changes ◽  
Ft Ir ◽  
Kinetics Of ◽  
Induced Structure ◽  
Ft Ir Spectroscopy

Steady-state and time-resolved FT-IR spectroscopy of site-specifically incorporated –SCN labels reveals local structure changes and kinetics of PYP after photo-excitation.

scholarly journals Rapid-scan FTIR difference spectroscopy applied to ubiquinone reduction in photosynthetic reaction centers: Role of redox mediators

2010 ◽  
Vol 24 (1-2) ◽  
pp. 79-87 ◽  
Author(s):  
Alberto Mezzetti
Keyword(s):  
Reaction Centers ◽  
Photosynthetic Reaction Centers ◽  
Difference Spectroscopy ◽  
Redox Mediators ◽  
Time Resolved ◽  
Rapid Scan ◽  
Primary Donor ◽  
Ftir Difference Spectroscopy ◽  
Kinetics Of

Rapid-scan FTIR difference spectroscopy was used to investigate light-induced reduction of the ubiquinone QB, and the oxidation kinetics of QB–and QH2by external mediators in isolated reaction centers (RCs) fromR. sphaeroides. As redox mediators, a Ferrocyanide/N,N,Nʹ,Nʹ-tetramethyl-p-phenylenediamine (TMPD) mixture and an Ascorbate/2,3,5,6-tetramethyl-p-phenylenediamine (DAD) mixture are compared.Results show that TMPDredrapidly reduces the photoproduced P870+primary donor. The process is fast enough to record rapid-scan FTIR spectra devoid of P870+bands down to 260 K. Results show also that TMPDoxoxidises both QB–and QH2faster than DADox. In particular, QB–is oxidised faster than QH2at all temperatures studied.Results are discussed in the framework of time-resolved infrared studies onR. sphaeroidesRCs, showing advantages/drawbacks of the proposed experimental approach.

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

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