Kinetics analysis of the electron transfer from nano-TiO2 to O2 through on-line absorptions and theoretical modeling

2021 ◽  
Vol 129 (16) ◽  
pp. 165106
Author(s):  
Baoshun Liu ◽  
Zhizhou Wu ◽  
Liuyang Li
Keyword(s):  
Electron Transfer ◽  
Theoretical Modeling ◽  
Kinetics Analysis ◽  
Nano Tio2 ◽  
On Line

Theoretical Modeling of Enzyme Reaction Chemistry:  The Electron Transfer of the Reduction Mechanism in CuZn Superoxide Dismutase

2004 ◽  
Vol 108 (41) ◽  
pp. 16255-16260 ◽  
Author(s):  
Maira D'Alessandro ◽  
Massimiliano Aschi ◽  
Maurizio Paci ◽  
Alfredo Di Nola ◽  
Andrea Amadei
Keyword(s):  
Electron Transfer ◽  
Superoxide Dismutase ◽  
Enzyme Reaction ◽  
Theoretical Modeling ◽  
Reduction Mechanism ◽  
Cuzn Superoxide Dismutase

scholarly journals Redox modulation of Low-Volume (100 µL) Solutions for XAFS measurements

2014 ◽  
Vol 70 (a1) ◽  
pp. C1523-C1523
Author(s):  
Stephen Best ◽  
M. Tauhid Islam ◽  
Christopher Chantler ◽  
Jay Bourke
Keyword(s):  
Electron Transfer ◽  
Structural Changes ◽  
Structural Information ◽  
Computational Techniques ◽  
Detailed Knowledge ◽  
Structural Reorganization ◽  
Redox States ◽  
Information Sampling ◽  
On Line ◽  
Low Volume

A key to the understanding of transition metal catalysis is a detailed knowledge of the changes in coordination environment that accompany a change in redox state. The capacity of a given metal complex to support the high rates of electron transfer needed for effective catalysis is strongly dependent on the magnitude of structural reorganization coupled to the redox step. The ability of the ligand to control the dynamics of electron transfer is beautifully illustrated by copper redox proteins such as plastocyanin.[1] The polypeptide-imposed constraints on the environment at the coordination site of the metal minimize the structural change attendant on interconversion between the CuI and CuII redox states of the metal, facilitating fast electron transfer. Further, unravelling the molecular details of enzyme catalysis often hinges on knowledge of the structural changes attendant on oxidation or reduction. XAFS can provide the key structural information for reactive or unstable redox states of biological and abiological molecules. Our research has mostly centred on the use of a combination of spectroscopic and computational techniques to reveal the chemistry associated with dihydrogen activation in diiron compounds related to [FeFe]-hydrogenases [2], where a combination of XAFS, IR spectroscopy and theory can provide reliable structural information. Sampling of such species can provide a comparable challenge to spectral analysis – an issue made more difficult in cases where the quantity of sample is limited. We have developed low-volume electrosynthesis cells suitable for the study of electrogenerated species where the total volume of solution required for XAS data collection is of order 100 µL [3]. The design and operation of cells designed to allow freeze quenching and tow-temperature spectral collection or RT on-line measurement will be described.

Kinetics and energetic analysis of the slow dispersive electron transfer from nano-TiO2 to O2 by in situ diffusion reflectance and Laplace transform

2021 ◽  
Author(s):  
Zhizhou Wu ◽  
Liuyang Li ◽  
Xuedong Zhou ◽  
Xiujian Zhao ◽  
Baoshun Liu
Keyword(s):  
Electron Transfer ◽  
Laplace Transform ◽  
Energy Distribution ◽  
Nano Tio2 ◽  
Barrier Energy ◽  
Energetic Analysis ◽  
In Situ Diffusion

In situ diffusion reflectances reveal the trapping-filling effect in the electron transfer from TiO2 to O2 and Laplace transform was developed to derive the broadened apparent barrier energy distribution.

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