English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

An efficient and selective four-electron plus four-proton (4e(-)/4H(+)) reduction of O(2) to water by decamethylferrocene and trifluoroacetic acid can be catalyzed by a synthetic analog of the heme a(3)/Cu(B) site in cytochrome c oxidase ((6)LFeCu) or its Cu-free version ((6)LFe) in acetone. A detailed mechanistic-kinetic study on the homogeneous catalytic system reveals spectroscopically detectable intermediates and that the rate-determining step changes from the O(2)-binding process at 25 °C room temperature (RT) to the O-O bond cleavage of a newly observed Fe(III)-OOH species at lower temperature (-60 °C). At RT, the rate of O(2)-binding to (6)LFeCu is significantly faster than that for (6)LFe, whereas the rates of the O-O bond cleavage of the Fe(III)-OOH species observed (-60 °C) with either the (6)LFeCu or (6)LFe catalyst are nearly the same. Thus, the role of the Cu ion is to assist the heme and lead to faster O(2)-binding at RT. However, the proximate Cu ion has no effect on the O-O bond cleavage of the Fe(III)-OOH species at low temperature.

Homogeneous catalytic O 2 reduction to water by a cytochrome c oxidase model with trapping of intermediates and mechanistic insights

Homogeneous catalytic O ₂ reduction to water by a cytochrome c oxidase model with trapping of intermediates and mechanistic insights