Surface enhanced resonance Raman spectroscopy of iron Hangman complexes on electrodes during electrocatalytic oxygen reduction: advantages and problems of common drycast methods.

about

Surface enhanced resonance Raman spectroscopy of iron Hangman complexes on electrodes during electrocatalytic oxygen reduction: advantages and problems of common drycast methods.

Item

http://www.wikidata.org/entity/Q53476337

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Surface enhanced resonance Ram ...... ems of common drycast methods.

@en

Surface enhanced resonance Ram ...... ems of common drycast methods.

@nl

type

Item

label

Surface enhanced resonance Ram ...... ems of common drycast methods.

@en

Surface enhanced resonance Ram ...... ems of common drycast methods.

@nl

prefLabel

Surface enhanced resonance Ram ...... ems of common drycast methods.

@en

Surface enhanced resonance Ram ...... ems of common drycast methods.

@nl

P1476

Surface enhanced resonance Ram ...... ems of common drycast methods.

@en

P2093

H K Ly

http://www.w3.org/2001/XMLSchema#string

M Schwalbe

http://www.w3.org/2001/XMLSchema#string

P Wrzolek

http://www.w3.org/2001/XMLSchema#string

R Götz

http://www.w3.org/2001/XMLSchema#string

P2860

A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

Porphyrin-Based Metal-Organic Frameworks as Heterogeneous Catalysts in Oxidation Reactions

Formation of mu-oxo dimer by the reaction of (meso-tetraphenylporphyrinato)iron(III) with various imidazoles.

Catalytic O[bond]O activation chemistry mediated by iron hangman porphyrins with a wide range of proton-donating abilities.

Surface Enhanced Resonance Raman Spectroscopy Reveals Potential Induced Redox and Conformational Changes of Cytochrome c Oxidase on Electrodes.

Proton-coupled electron transfer: a unifying mechanism for biological charge transport, amino acid radical initiation and propagation, and bond making/breaking reactions of water and oxygen.

Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase.

Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin.

Role of proton-coupled electron transfer in O-O bond activation.

Direct observation of intermediates formed during steady-state electrocatalytic O2 reduction by iron porphyrins.

P304

13220-13228

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1039/C7DT01174A

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Inez Weidinger

P577

2017-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28682383

http://www.w3.org/2001/XMLSchema#string