Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.

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Molecular details of multielectron transfer: the case of multiheme cytochromes from metal respiring organisms.

P2860

Q37737573-11672F35-895E-4820-957D-7CEFFE7FA3AC

P2860

Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.

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http://www.wikidata.org/entity/Q45175198

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2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

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Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

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type

Item

label

Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

@en

Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

@nl

prefLabel

Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

@en

Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

@nl

P1476

Redox behaviour of the haem do ...... a frigidimarina probed by NMR.

@en

P2093

António V Xavier

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

Caroline S Miles

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

Emma L Rothery

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

Graeme A Reid

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

Miguel Pessanha

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

Stephen K Chapman

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P2860

Structural and mechanistic mapping of a unique fumarate reductase

Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study

Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina

Engineering water to act as an active site acid catalyst in a soluble fumarate reductase

Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina

NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation.

Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.

Electron-transfer mechanisms through biological redox chains in multicenter enzymes.

Structure-function relationship in type II cytochrome c(3) from Desulfovibrio africanus: a novel function in a familiar heme core.

A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis.

P304

185-190

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P31

scholarly article

P356

10.1016/J.FEBSLET.2004.10.098

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P407

English

P433

1-2

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

P478

578

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P50

Carlos A. Salgueiro

David L. Turner

Ricardo O Louro

P577

2004-12-01T00:00:00Z

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

P5875

8145551

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

P698

15581639

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Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.

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P2860

P2860

Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698