Probing electrostatic interactions in cytochrome c using site-directed chemical modification.

about

Probing electrostatic interactions in cytochrome c using site-directed chemical modification.

Item

http://www.wikidata.org/entity/Q43979199

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh-hant

name

Probing electrostatic interact ...... irected chemical modification.

@en

Probing electrostatic interact ...... irected chemical modification.

@nl

type

Item

label

Probing electrostatic interact ...... irected chemical modification.

@en

Probing electrostatic interact ...... irected chemical modification.

@nl

prefLabel

Probing electrostatic interact ...... irected chemical modification.

@en

Probing electrostatic interact ...... irected chemical modification.

@nl

P1476

Probing electrostatic interact ...... irected chemical modification.

@en

P2093

Carmichael J A Wallace

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

Christian Blouin

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

J Guy Guillemette

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

P2860

High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c

Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity

Spectroscopic analysis of the cytochrome c oxidase-cytochrome c complex: circular dichroism and magnetic circular dichroism measurements reveal change of cytochrome c heme geometry imposed by complex formation.

Internal and interfacial dielectric properties of cytochrome c from molecular dynamics in aqueous solution.

Definition of the interaction domain for cytochrome c on the cytochrome bc(1) complex. Steady-state and rapid kinetic analysis of electron transfer between cytochrome c and Rhodobacter sphaeroides cytochrome bc(1) surface mutants.

Oxidation of cytochrome c by cytochrome c oxidase: spectroscopic binding studies and steady-state kinetics support a conformational transition mechanism.

On the relationship between oxidation-reduction potential and biological activity in cytochrome c analogues. Results from four novel two-fragment complexes.

Protein matrix and dielectric effect in cytochrome c.

Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins.

Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: a resonance Raman study.

P304

197-203

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

P31

scholarly article

P356

10.1139/O01-238

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

P433

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

P478

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

P577

2002-01-01T00:00:00Z

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

P698

11989715

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