Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 428069
Title Cofactor binding protects flavodoxin against oxidative stress
Author(s) Lindhoud, S.; Berg, W.A.M. van den; Heuvel, R.H.H. van den; Heck, A.J.R.; Mierlo, C.P.M. van; Berkel, W.J.H. van
Source PLoS One 7 (2012)7. - ISSN 1932-6203
DOI https://doi.org/10.1371/journal.pone.0041363
Department(s) Biochemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) methionine sulfoxide reductase - azotobacter-vinelandii apoflavodoxin - para-hydroxybenzoate hydroxylase - alkyl hydroperoxide reductase - cysteine sulfinic acid - beta parallel protein - sulfenic acid - pseudomonas-fluorescens - hydrogen-peroxide - mass-spectrome
Abstract In organisms, various protective mechanisms against oxidative damaging of proteins exist. Here, we show that cofactor binding is among these mechanisms, because flavin mononucleotide (FMN) protects Azotobacter vinelandii flavodoxin against hydrogen peroxide-induced oxidation. We identify an oxidation sensitive cysteine residue in a functionally important loop close to the cofactor, i.e., Cys69. Oxidative stress causes dimerization of apoflavodoxin (i.e., flavodoxin without cofactor), and leads to consecutive formation of sulfinate and sulfonate states of Cys69. Use of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) reveals that Cys69 modification to a sulfenic acid is a transient intermediate during oxidation. Dithiothreitol converts sulfenic acid and disulfide into thiols, whereas the sulfinate and sulfonate forms of Cys69 are irreversible with respect to this reagent. A variable fraction of Cys69 in freshly isolated flavodoxin is in the sulfenic acid state, but neither oxidation to sulfinic and sulfonic acid nor formation of intermolecular disulfides is observed under oxidising conditions. Furthermore, flavodoxin does not react appreciably with NBD-Cl. Besides its primary role as redox-active moiety, binding of flavin leads to considerably improved stability against protein unfolding and to strong protection against irreversible oxidation and other covalent thiol modifications. Thus, cofactors can protect proteins against oxidation and modification
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