Heteroditopic Ligand Accommodating a Fused Phenanthroline and a Schiff Base Cavity as Molecular Spacer in the Study of Electron and Energy Transfer

2005 ◽  
Vol 11 (12) ◽  
pp. 3698-3710 ◽  
Author(s):  
Yann Pellegrin ◽  
Annamaria Quaranta ◽  
Pierre Dorlet ◽  
Marie France Charlot ◽  
Winfried Leibl ◽  
...  
Keyword(s):  
Schiff Base ◽  
Energy Transfer ◽  
Base Cavity

scholarly journals Synthesis and characterization of novel porphyrin Schiff bases

2008 ◽  
Vol 73 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Lei Wang ◽  
Yaqing Feng ◽  
Jinqiang Xue ◽  
Li Yukun
Keyword(s):  
Schiff Base ◽  
Energy Transfer ◽  
Spectral Data ◽  
Schiff Bases ◽  
Chemical Properties ◽  
Synthesis And Characterization ◽  
Intramolecular Energy Transfer ◽  
Porphyrin Moiety

Novel porphyrin Schiff bases were synthesized by a simple Schiff base condensation in refluxing toluene between 5-(4-aminophenyl)-10,15,20-triphe?nylporphyrin (ATTP) 3 and styryl aldehydes 4-6 or p-halobenzaldehydes 7-9. The newly synthesized porphyrin Schiff bases were characterized on the basis of their chemical properties and spectral data. A good intramolecular energy transfer from the styryl unit to the porphyrin moiety was found.

scholarly journals High-resolution structural insights into the heliorhodopsin family

2020 ◽  
Vol 117 (8) ◽  
pp. 4131-4141 ◽  
Author(s):  
K. Kovalev ◽  
D. Volkov ◽  
R. Astashkin ◽  
A. Alekseev ◽  
I. Gushchin ◽  
...  
Keyword(s):  
Schiff Base ◽  
Bioinformatic Analysis ◽  
Proton Acceptor ◽  
Water Molecules ◽  
Primary Proton ◽  
Biological Processes ◽  
New Family ◽  
Charged Amino Acids ◽  
Base Cavity ◽  
Structural Insights

Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 Å, which highlight its remarkable difference from all known rhodopsins. The interior of HeR’s extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes.

A quantitative approach to inner shell losses

1978 ◽  
Vol 36 (1) ◽  
pp. 526-527 ◽  
Author(s):  
R.D. Leapman ◽  
P. Rez ◽  
D.F. Mayers
Keyword(s):  
Energy Transfer ◽  
Cross Section ◽  
Cross Sections ◽  
Accurate Determination ◽  
Background Intensity ◽  
Core Excitation ◽  
Quantitative Basis ◽  
Cross Section Differential ◽  
Bound Electrons

Microanalysis by EELS has been developing rapidly and though the general form of the spectrum is now understood there is a need to put the technique on a more quantitative basis (1,2). Certain aspects important for microanalysis include: (i) accurate determination of the partial cross sections, σx(α,ΔE) for core excitation when scattering lies inside collection angle a and energy range ΔE above the edge, (ii) behavior of the background intensity due to excitation of less strongly bound electrons, necessary for extrapolation beneath the signal of interest, (iii) departures from the simple hydrogenic K-edge seen in L and M losses, effecting σx and complicating microanalysis. Such problems might be approached empirically but here we describe how computation can elucidate the spectrum shape.The inelastic cross section differential with respect to energy transfer E and momentum transfer q for electrons of energy E0 and velocity v can be written as

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