Search: WFRF:(Wolf Christiane) >
Extraordinary μs-ms...
Extraordinary μs-ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q
-
- Ådén, Jörgen, 1980- (author)
- Umeå universitet,Kemiska institutionen
-
- Wallgren, Marcus, 1978- (author)
- Umeå universitet,Kemiska institutionen
-
- Storm, Patrik, 1966- (author)
- Umeå universitet,Kemiska institutionen
-
show more...
-
- Weise, Christoph, 1973- (author)
- Umeå universitet,Kemiska institutionen
-
- Christiansen, Alexander, 1982- (author)
- Umeå universitet,Kemiska institutionen
-
- Schröder, Wolfgang P (author)
- Umeå universitet,Kemiska institutionen
-
- Funk, Christiane (author)
- Umeå universitet,Kemiska institutionen
-
- Wolf-Watz, Magnus, 1971- (author)
- Umeå universitet,Kemiska institutionen
-
show less...
-
(creator_code:org_t)
- Elsevier, 2011
- 2011
- English.
-
In: Biochimica et Biophysica Acta. - : Elsevier. - 0006-3002 .- 1878-2434. ; 1814:12, s. 1880-1890
- Related links:
-
https://urn.kb.se/re...
-
show more...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Peroxiredoxin Q (PrxQ) isolated from Arabidopsis thaliana belongs to a family of redox enzymes called peroxiredoxins, which are thioredoxin- or glutaredoxin-dependent peroxidases acting to reduce peroxides and in particular hydrogen peroxide. PrxQ cycles between an active reduced state and an inactive oxidized state during its catalytic cycle. The catalytic mechanism involves a nucleophilic attack of the catalytic cysteine on hydrogen peroxide to generate a sulfonic acid intermediate with a concerted release of a water molecule. This intermediate is subsequently relaxed by the reaction of a second cysteine, denoted the resolving cysteine, generating an intramolecular disulfide bond and release of a second water molecule. PrxQ is recycled to the active state by a thioredoxin-dependent reduction. Previous structural studies of PrxQ homologues have provided the structural basis for the switch between reduced and oxidized conformations. Here, we have performed a detailed study of the activity, structure and dynamics of PrxQ in both the oxidized and reduced states. Reliable and experimentally validated structural models of PrxQ in both oxidation states were generated using homology based modeling. Analysis of NMR spin relaxation rates shows that PrxQ is monomeric in both oxidized and reduced states. As evident from R(2) relaxation rates the reduced form of PrxQ undergoes unprecedented dynamics on the slow μs-ms timescale. The ground state of this conformational dynamics is likely the stably folded reduced state as implied by circular dichroism spectroscopy. We speculate that the extensive dynamics is intimately related to the catalytic function of PrxQ.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Keyword
- NMR
- Enzyme
- Dynamics
- Peroxiredoxin
- Arabidopsis thaliana
- Chemistry
- Kemi
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Ådén, Jörgen, 19 ...
-
Wallgren, Marcus ...
-
Storm, Patrik, 1 ...
-
Weise, Christoph ...
-
Christiansen, Al ...
-
Schröder, Wolfga ...
-
show more...
-
Funk, Christiane
-
Wolf-Watz, Magnu ...
-
show less...
- About the subject
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Chemical Science ...
- Articles in the publication
-
Biochimica et Bi ...
-
Biochimica et Bi ...
- By the university
-
Umeå University