Reduction of dioxygen to water by a Co(N2O2) complex with a 2,2′-bipyridine backbone

2021 ◽  
Author(s):  
Asa W. Nichols ◽  
Joseph S. Kuehner ◽  
Brittany L. Huffman ◽  
Peter R. Miedaner ◽  
Diane A. Dickie ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Intrinsic Activity ◽  
Dioxygen Reduction

The first Co(N2O2)-based catalyst with intrinsic activity for dioxygen reduction to water instead of hydrogen peroxide is reported.

Efficient hydrogen peroxide synthesis by metal-free polyterthiophene via photoelectrocatalytic dioxygen reduction

2020 ◽  
Vol 13 (1) ◽  
pp. 238-245 ◽  
Author(s):  
Wenjun Fan ◽  
Bingqing Zhang ◽  
Xiaoyu Wang ◽  
Weiguang Ma ◽  
Deng Li ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxygen Reduction ◽  
Cost Effective ◽  
High Concentration ◽  
Metal Free ◽  
Dioxygen Reduction ◽  
Polymeric Semiconductor ◽  
Hydrogen Peroxide Synthesis

We demonstrate the metal-free polymeric semiconductor pTTh as a selective and efficient photocathode for photoelectrochemical oxygen reduction to a high concentration of H2O2 in a cost-effective way.

Structure–activity relationship of nanostructured ceria for the catalytic generation of hydroxyl radicals

Nanoscale ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 4552-4561 ◽  
Author(s):  
Tamra J. Fisher ◽  
Yunyun Zhou ◽  
Tai-Sing Wu ◽  
Meiyu Wang ◽  
Yun-Liang Soo ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Hydroxyl Radicals ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Intrinsic Activity ◽  
Atomic Structures ◽  
Structure Activity ◽  
Nanostructured Ceria ◽  
Ceria Catalysts ◽  
Relationship Of

The morphologies and associated atomic structures of ceria catalysts influence their intrinsic activity towards the catalytic production of hydroxyl radicals from hydrogen peroxide.

Intrinsic Activity of Metal Centers in Metal–Nitrogen–Carbon Single-Atom Catalysts for Hydrogen Peroxide Synthesis

2020 ◽  
Vol 142 (52) ◽  
pp. 21861-21871
Author(s):  
Chang Liu ◽  
Hao Li ◽  
Fei Liu ◽  
Junsheng Chen ◽  
Zixun Yu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Single Atom ◽  
Intrinsic Activity ◽  
Metal Centers ◽  
Hydrogen Peroxide Synthesis

The Mechanism of Dioxygen Reduction at Iron meso-Tetrakis (Pyridyl) Porphyrin: a Spectroelectrochemical Study

1998 ◽  
Vol 02 (03) ◽  
pp. 249-260 ◽  
Author(s):  
S. POPOVICI ◽  
W. LEYFFER ◽  
R. HOLZE
Keyword(s):  
Hydrogen Peroxide ◽  
Cyclic Voltammetry ◽  
Strong Influence ◽  
Resonance Raman ◽  
Reduction Reaction ◽  
Reduction Product ◽  
Dioxygen Reduction ◽  
Primary Reduction

The mechanism of the dioxygen interaction with and reduction reaction at iron α,β,γ,δ-tetra(4-pyridyl) porphyrin ( FeTPyP ) deposited on carbon and silver supporting electrodes was investigated with cyclic voltammetry and FTIR, UV-vis and resonance Raman spectroscopies. Results indicate a strong influence of the ligand upon the reduction electrocatalysis. Spectroelectrochemical results support a two-electron pathway resulting most probably in hydrogen peroxide as the primary reduction product.

Introduction of Secondary Ligand in Titanium-Based Metal-Organic Frameworks for Visible-Light-Driven Photocatalytic Hydrogen Peroxide Production from Dioxygen Reduction

2021 ◽  
Author(s):  
Xiaolang Chen ◽  
Yasutaka Kuwahara ◽  
Kohsuke Mori ◽  
Catherine Louis ◽  
Hiromi Yamashita
Keyword(s):  
Hydrogen Peroxide ◽  
Visible Light ◽  
Catalytic Properties ◽  
Metal Organic Frameworks ◽  
Hydrogen Peroxide Production ◽  
Multiple Components ◽  
Dioxygen Reduction ◽  
Visible Light Driven ◽  
Metal Organic ◽  
Secondary Ligand

Introduction of multiple components with specific properties in metal–organic frameworks (MOFs) is an attractive strategy to modify their catalytic properties. Herein, through the introduction of ligand 4,4’,4’’,4’’’-(pyrene-1,3,6,8-tetrayl)tetrabenzoic acid (L2) in...

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

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