scholarly journals Conformational States of Cytochrome P450 Oxidoreductase Evaluated by Förster Resonance Energy Transfer Using Ultrafast Transient Absorption Spectroscopy

Biochemistry ◽  
2016 ◽  
Vol 55 (43) ◽  
pp. 5973-5976 ◽  
Author(s):  
Elizaveta A. Kovrigina ◽  
Brian Pattengale ◽  
Chuanwu Xia ◽  
Azamat R. Galiakhmetov ◽  
Jier Huang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Energy Transfer ◽  
Absorption Spectroscopy ◽  
Transient Absorption ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Transient Absorption Spectroscopy ◽  
Conformational States ◽  
P450 Oxidoreductase ◽  
Cytochrome P450 Oxidoreductase

Dynamic receptor superstructures at the plasma membrane

1997 ◽  
Vol 30 (1) ◽  
pp. 67-106 ◽  
Author(s):  
S. DAMJANOVICH ◽  
R. GÁSPÁR, Jr. ◽  
C. PIERI
Keyword(s):  
Plasma Membrane ◽  
Energy Transfer ◽  
Single Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Scanning Force Microscopy ◽  
Physical Parameters ◽  
Conformational States ◽  
Lipid Domain ◽  
Receptor Clusters

1. INTRODUCTION 681.1 Receptor patterns in the plasma membrane 681.2 Different types of receptor patterns 712. METHODS TO INVESTIGATE NON-RANDOM RECEPTOR CLUSTERING 732.1 Fluorescence resonance energy transfer 732.2 Flow cytometric energy transfer measurement 782.3 Fluorescence anisotropy and energy transfer 792.4 Photobleaching energy transfer on single cells 812.5 Two-dimensional mapping of receptor superstructures 822.6 Detecting single receptor molecules 852.7 Chemical identification of receptor clusters 862.8 Electron microscopy 872.9 Scanning force microscopy 883. CONFORMATIONAL STATES OF RECEPTORS 903.1 Multi-subunit receptor structures 903.2 Physical parameters influencing conformational states 913.3 Chemical interactions and receptor conformations 924. ON THE ORIGIN OF NATURALLY OCCURRING RECEPTOR CLUSTERS 934.1 Synthesis of receptors and their localization in the plasma membrane 934.2 Lipid domain structure of the plasma membrane 944.3 The validity of the Singer–Nicolson model 945. CONCLUSIONS 966. ACKNOWLEDGEMENTS 967. REFERENCES 97

Decoupling the artificial special pair to slow down the rate of singlet energy transfer

2012 ◽  
Vol 16 (05n06) ◽  
pp. 685-694 ◽  
Author(s):  
Pierre D. Harvey ◽  
Adam Langlois ◽  
Mikhail Filatov ◽  
Daniel Fortin ◽  
Kei Ohkubo ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Absorption Spectroscopy ◽  
Density Functional ◽  
Transient Absorption ◽  
Geometry Optimization ◽  
Transient Absorption Spectroscopy ◽  
Free Base ◽  
Functional Theory ◽  
Time Resolved ◽  
Slow Rise

Trimer 2, composed of a cofacial heterobismacrocycle, octamethyl-porphyrin zinc(II) and bisarylporphyrin zinc(II) held by an anthracenyl spacer, and a flanking acceptor, bisarylporphyrin free-base ( Ar = -3,5-(t Bu )2 C 6 H 3), has been studied by means of absorption spectroscopy, "steady state and time-resolved fluorescence" and fs transient absorption spectroscopy, and density functional theory (DFT) in order to assess the effect of decoupling the chromophores' low energy MOs on the rate of the singlet, S1, energy transfer, k ET , compared to a recently reported work on a heavily coupled trimeric system, Trimer 1, [biphenylenebis(n-nonyl)porphyrin zinc(II)]-bisarylporphyrin free-base ( Ar = -3,5-(t Bu )2 C 6 H 3). The position of the 0–0 peaks of the absorption and fluorescence spectra of Trimer 2 indicates that these porphyrin units are respectively energy donor 1, donor 2, and acceptor. The DFT computations confirm that the MOs of the cofacial donor 1-donor 2 dyad are decoupled, but significant MO coupling between donor 2 and acceptor 1 is still present despite the strong dihedral angle between their respective average planes (77.5°: geometry optimization by DFT). The fs transient absorption spectra exhibit a clear S1–Sn fingerprint of the bisarylporphyrin zinc(II) chromophore and the kinetic trace exhibits a slow rise time of 87 ps, due to a S1 donor 1 → donor 2 ET. The transient species donor 2 and acceptor decay respectively in the short (~1.5) ns and 6 ns time scale.

scholarly journals A Large-Scale Allosteric Transition in Cytochrome P450 3A4 Revealed by Luminescence Resonance Energy Transfer (LRET)

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e83898 ◽  
Author(s):  
Elena V. Sineva ◽  
Jessica A. O. Rumfeldt ◽  
James R. Halpert ◽  
Dmitri R. Davydov
Keyword(s):  
Cytochrome P450 ◽  
Energy Transfer ◽  
Large Scale ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Cytochrome P450 3A4 ◽  
Allosteric Transition

Energy transfer within pc trimers of mastigocladus laminosus studied by picosecond time-resolved transient absorption spectroscopy

1988 ◽  
Vol 43 (1-2) ◽  
pp. 55-62 ◽  
Author(s):  
S. Schneider ◽  
P. Geiselhart ◽  
S. Siebzehnrübl ◽  
R. Fischer ◽  
H. Scheer
Keyword(s):  
Energy Transfer ◽  
Least Squares ◽  
Absorption Spectroscopy ◽  
Transient Absorption ◽  
Transient Absorption Spectroscopy ◽  
Transfer Time ◽  
Acceptor State ◽  
Time Resolved ◽  
Picosecond Pulses ◽  
Exponential Fit

The transient absorption recovery induced in phycocyanin trimers by picosecond pulses of variable wavelength (570-620 nm) has been recorded and analyzed by applying a least-squares multi-exponential fit procedure. The results suggest that in native PC trimers the chromophores exhibit a microheterogeneity with the effect that the derived apparent lifetimes are functions of excitation and probing wavelength. It is suggested that, due to strong excitonic coupling between a-84 and β-84 chromophores, the lifetime of the terminal acceptor state is reduced to about 900 ps; the apparent energy transfer time from chromophore β-155 to a-84 and β-84 chromophores varies between 20-50 ps depending on the actual chromophore-protein arrangement (microheterogeneity)

Distinguishing Förster resonance energy transfer and solvent-mediated charge-transfer relaxation dynamics in a zinc(ii) indicator: a femtosecond time-resolved transient absorption spectroscopic study

2014 ◽  
Vol 16 (11) ◽  
pp. 5088-5092 ◽  
Author(s):  
Kesavapillai Sreenath ◽  
Chongyue Yi ◽  
Kenneth L. Knappenberger ◽  
Lei Zhu
Keyword(s):  
Energy Transfer ◽  
Charge Transfer ◽  
Transient Absorption ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Solvent Polarity ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Relaxation Dynamics ◽  
Förster Resonance

The rates of intramolecular Förster resonance energy transfer and solvent-mediated relaxation of charge-transfer excited state have oppsite solvent polarity dependencies.

scholarly journals Ligand‐induced conformational changes in cytochrome P450 3A4 detected by luminescence resonance energy transfer (LRET)

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Elena V Sineva ◽  
Jessica Rumfeldt ◽  
Anastasia Yu Bakulina ◽  
James R Halpert ◽  
Dmitri R Davydov
Keyword(s):  
Cytochrome P450 ◽  
Energy Transfer ◽  
Conformational Changes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Cytochrome P450 3A4
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