Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
about
Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.Acid/base triggered interconversion of μ-η2:η2-peroxido and bis(μ-oxido) dicopper intermediates capped by proton-responsive ligands.A High-Valent Non-Heme μ-Oxo Manganese(IV) Dimer Generated from a Thiolate-Bound Manganese(II) Complex and Dioxygen.On the Way to a Trisanionic {Cu3 O2 } Core for Oxidase Catalysis: Evidence of an Asymmetric Trinuclear Precursor Stabilized by Perfluoropinacolate Ligands.The teleos of metallo-reduction and metallo-oxidation in eukaryotic iron and copper trafficking.Oxygen Delivery as a Limiting Factor in Modelling Dicopper(II) Oxidase Reactivity.
P2860
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
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2016年學術文章
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2016年學術文章
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name
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@en
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@nl
type
label
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@en
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@nl
prefLabel
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@en
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@nl
P2860
P1433
P1476
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
@en
P2860
P304
P356
10.1021/ACS.INORGCHEM.6B01034
P407
P577
2016-06-14T00:00:00Z