Reconstitution of supramolecular organization involved in energy metabolism at electrochemical interfaces for biosensing and bioenergy production.

about

Spectroscopic characterization of a green copper site in a single-domain cupredoxin Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation.Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin.

P2860

Q28539714-91AA570B-F1DB-46F2-89BF-E98DA5B0ABC8 Q37380010-D3508027-4DD5-4D19-AAD5-F92E3C50D18B Q55390226-E09CECAD-4532-4785-A243-098584AE925D

P2860

Reconstitution of supramolecular organization involved in energy metabolism at electrochemical interfaces for biosensing and bioenergy production.

Item

http://www.wikidata.org/entity/Q38167617

description

article científic

@ca

article scientifique

@fr

articol științific

@ro

articolo scientifico

@it

artigo científico

@gl

artigo científico

@pt

artigo científico

@pt-br

artikel ilmiah

@id

artikull shkencor

@sq

artículo científico

@es

name

Reconstitution of supramolecul ...... sing and bioenergy production.

@en

type

Item

label

Reconstitution of supramolecul ...... sing and bioenergy production.

@en

prefLabel

Reconstitution of supramolecul ...... sing and bioenergy production.

@en

P1476

Reconstitution of supramolecul ...... sing and bioenergy production.

@en

P2093

E Lojou

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

M Guiral

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

M Roger

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

M T Giudici-Orticoni

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

P2860

A new iron-oxidizing/O2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans

High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways

Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å

Bilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reduction

Microbial ecology meets electrochemistry: electricity-driven and driving communities

A membrane-bound multienzyme, hydrogen-oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

Direct electrochemistry of cytochrome c on a phosphonic acid terminated self-assembled monolayers.

Probing electron transfer mechanisms in Shewanella oneidensis MR-1 using a nanoelectrode platform and single-cell imaging.

The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway.

P2888

s00216-013-7465-1

P304

1011-1027

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

P31

scholarly article

P356

10.1007/S00216-013-7465-1

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

P407

English

P433

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

P478

406

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

P50

Alexandre Ciaccafava

Marianne Ilbert

Anne de Poulpiquet

P577

2013-12-01T00:00:00Z

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

P5875

259110234

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

P698

24292430

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

P921

electrochemistry

Reconstitution of supramolecular organization involved in energy metabolism at electrochemical interfaces for biosensing and bioenergy production.

about

P2860

P2860

Reconstitution of supramolecular organization involved in energy metabolism at electrochemical interfaces for biosensing and bioenergy production.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921