Evidence for a novel mechanism of time-resolved flavin fluorescence depolarization in glutathione reductase.
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Molecular eyes: proteins that transform light into biological informationNO formation by neuronal NO-synthase can be controlled by ultrafast electron injection from a nanotrigger.Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.Redox modulation of flavin and tyrosine determines photoinduced proton-coupled electron transfer and photoactivation of BLUF photoreceptors.Structural changes of yellow Cameleon domains observed by quantitative FRET analysis and polarized fluorescence correlation spectroscopy.Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.Real-time enzyme dynamics illustrated with fluorescence spectroscopy of p-hydroxybenzoate hydroxylase.Sensitive fluorescence-based detection of magnetic field effects in photoreactions of flavins.
P2860
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P2860
Evidence for a novel mechanism of time-resolved flavin fluorescence depolarization in glutathione reductase.
description
2004 nî lūn-bûn
@nan
2004年の論文
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2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Evidence for a novel mechanism ...... tion in glutathione reductase.
@en
type
label
Evidence for a novel mechanism ...... tion in glutathione reductase.
@en
prefLabel
Evidence for a novel mechanism ...... tion in glutathione reductase.
@en
P2093
P2860
P1433
P1476
Evidence for a novel mechanism ...... tion in glutathione reductase.
@en
P2093
Antonie J W G Visser
Arie van Hoek
Petra A W van den Berg
P2860
P304
P356
10.1529/BIOPHYSJ.104.040030
P407
P577
2004-10-01T00:00:00Z