2010
DOI: 10.1021/ja1020519
|View full text |Cite
|
Sign up to set email alerts
|

When Is the Helix Conformation Restored after the Reverse Reaction of Phototropin?

Abstract: Following the disruption of the covalent bond between the cysteine and flavin of Phot1LOV2-linker, the unfolded conformation of the linker folds with a time constant of 13 ms, which is considerably (approximately 10(4) times) slower than the helix formation rate measured for an alpha-helical polypeptide in solution.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
6
0

Year Published

2011
2011
2021
2021

Publication Types

Select...
6
1

Relationship

1
6

Authors

Journals

citations
Cited by 8 publications
(6 citation statements)
references
References 21 publications
0
6
0
Order By: Relevance
“…This may be due to probe light‐induced acceleration of thermal recovery in these proteins as the 1.8‐ANS fluorescence has to be excited at relatively short wavelength ( i.e. 350 nm; compare [26,27]).…”
Section: Resultsmentioning
confidence: 99%
“…This may be due to probe light‐induced acceleration of thermal recovery in these proteins as the 1.8‐ANS fluorescence has to be excited at relatively short wavelength ( i.e. 350 nm; compare [26,27]).…”
Section: Resultsmentioning
confidence: 99%
“…Time-resolved nuclear magnetic resonance (NMR) spectroscopy on the isolated LOV2 domain from Avena sativa phototropin1 has revealed a difference between the mean time constant resulting from NMR studies and the lifetime of the adduct state by a factor of 1.2, but in the time region of seconds 38 . Moreover, the recovery of the LOV2-linker from Arabidopsis takes place rapidly with a 13 ms time constant according to transient grating experiments 39 . A difference on the time scale of minutes has only been reported previously for a LOV domain with flanking helices, PpSB1-LOV-R66I from Pseudomonas putida , by time-course SAXS experiments 22 …”
Section: Discussionmentioning
confidence: 99%
“…Thus, absorption of blue light leads to the transient formation of a covalent bond between the FMN cofactor and the protein, which slowly ruptures in the dark to regenerate the noncovalent dark ground state species, presumably through a base‐catalyzed mechanism (33,34). Absorption of near‐UV light may also rupture the covalent adduct (35,36). Formation of a covalent bond to FMN bond triggers protein conformational changes on the surface of the PAS core which weaken interactions of this core with a C‐terminal amphiphilic helix called Jα, packed against its central β‐sheet (37–39).…”
Section: Introductionmentioning
confidence: 99%