Voltammetric Sensing of Soybean Agglutinin Using an Electrode Modified with Electron‐Transfer, Carbohydrate‐Mimetic/Cross‐Linker‐Peptide‐Collagen Film

2021 ◽  
Author(s):  
Sora Ishizaki ◽  
Hideki Kuramitz ◽  
Kazuharu Sugawara
2020 ◽  
Vol 1116 ◽  
pp. 53-61
Author(s):  
Kazuharu Sugawara ◽  
Sora Ishizaki ◽  
Keito Kodaira ◽  
Hideki Kuramitz ◽  
Toshihiko Kadoya

RSC Advances ◽  
2020 ◽  
Vol 10 (42) ◽  
pp. 25402-25407
Author(s):  
Xiaodong Lv ◽  
Peng Gao

Based on the electron-transfer mechanism between the template and quantum dots (QDs), an optical sensor was structured.


RSC Advances ◽  
2014 ◽  
Vol 4 (49) ◽  
pp. 25675-25682 ◽  
Author(s):  
Madhu Tiwari ◽  
Sandeep Gupta ◽  
Rajiv Prakash

The synthesized coordination polymer DMTD–Au has a layered structure, in which the layers are stacked via π–π stacking and hydrophobic interaction. It facilitates electron transfer kinetics, which has been utilized in the ultra trace sensing of resorcinol.


Author(s):  
P. Bonhomme ◽  
A. Beorchia

We have already described (1.2.3) a device using a pockel's effect light valve as a microscopical electron image converter. This converter can be read out with incoherent or coherent light. In the last case we can set in line with the converter an optical diffractometer. Now, electron microscopy developments have pointed out different advantages of diffractometry. Indeed diffractogram of an image of a thin amorphous part of a specimen gives information about electron transfer function and a single look at a diffractogram informs on focus, drift, residual astigmatism, and after standardizing, on periods resolved (4.5.6). These informations are obvious from diffractogram but are usualy obtained from a micrograph, so that a correction of electron microscope parameters cannot be realized before recording the micrograph. Diffractometer allows also processing of images by setting spatial filters in diffractogram plane (7) or by reconstruction of Fraunhofer image (8). Using Electrotitus read out with coherent light and fitted to a diffractometer; all these possibilities may be realized in pseudoreal time, so that working parameters may be optimally adjusted before recording a micrograph or before processing an image.


2004 ◽  
Vol 71 ◽  
pp. 1-14
Author(s):  
David Leys ◽  
Jaswir Basran ◽  
François Talfournier ◽  
Kamaldeep K. Chohan ◽  
Andrew W. Munro ◽  
...  

TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring flavoprotein). The mechanism of electron transfer between TMADH and ETF has been studied using stopped-flow kinetic and mutagenesis methods, and more recently by X-ray crystallography. Potentiometric methods have also been used to identify key residues involved in the stabilization of the flavin radical semiquinone species in ETF. These studies have demonstrated a key role for 'conformational sampling' in the electron-transfer complex, facilitated by two-site contact of ETF with TMADH. Exploration of three-dimensional space in the complex allows the FAD of ETF to find conformations compatible with enhanced electronic coupling with the 4Fe-4S centre of TMADH. This mechanism of electron transfer provides for a more robust and accessible design principle for interprotein electron transfer compared with simpler models that invoke the collision of redox partners followed by electron transfer. The structure of the TMADH-ETF complex confirms the role of key residues in electron transfer and molecular assembly, originally suggested from detailed kinetic studies in wild-type and mutant complexes, and from molecular modelling.


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