K
Karolien Van Belle
Researcher at Vrije Universiteit Brussel
Publications - 14
Citations - 601
Karolien Van Belle is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Arsenate reductase & Active site. The author has an hindex of 10, co-authored 14 publications receiving 557 citations. Previous affiliations of Karolien Van Belle include Flanders Institute for Biotechnology & VU University Amsterdam.
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Journal ArticleDOI
Arsenate Reductase, Mycothiol, and Mycoredoxin Concert Thiol/Disulfide Exchange
Efrén Ordóñez,Karolien Van Belle,Goedele Roos,Sandra De Galan,Michal Letek,José A. Gil,Lode Wyns,Luis M. Mateos,Joris Messens +8 more
TL;DR: The catalytic mechanism for the reduction of arsenate to arsenite in Corynebacterium glutamicum is unraveled, paving the way for the study of redox mechanisms in actinobacteria.
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Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria.
Koen Van Laer,Lieven Buts,Lieven Buts,Nicolas Foloppe,Didier Vertommen,Karolien Van Belle,Karolien Van Belle,Khadija Wahni,Khadija Wahni,Goedele Roos,Lennart Nilsson,Luis M. Mateos,Mamta Rawat,Nico A. J. van Nuland,Nico A. J. van Nuland,Joris Messens,Joris Messens +16 more
TL;DR: Determination of the oxidized and reduced structures of mycoredoxin‐1, better understanding of the mycothiol‐dependent reactions in general, will likely give new insights in how M. tuberculosis survives oxidative stress in human macrophages.
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The oxidase DsbA folds a protein with a nonconsecutive disulfide.
Joris Messens,Joris Messens,Jean-François Collet,Karolien Van Belle,Karolien Van Belle,Elke Brosens,Elke Brosens,Remy Loris,Remy Loris,Lode Wyns,Lode Wyns +10 more
TL;DR: Periplasmic ribonuclease I from Escherichia coli is presented as a new endogenous substrate for the study of oxidative protein folding and shows that DsbA is a sufficient catalyst for correct disulfide formation in vivo and in vitro.
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All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Joris Messens,José C. Martins,Karolien Van Belle,Elke Brosens,Aline Desmyter,Marjan De Gieter,Jean-Michel Wieruszeski,Rudolph Willem,Lode Wyns,Ingrid Zegers +9 more
TL;DR: The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled and Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis.
Journal ArticleDOI
The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.
Goedele Roos,Abel Garcia-Pino,Karolien Van Belle,Elke Brosens,Khadija Wahni,Guy Vandenbussche,Lode Wyns,Remy Loris,Joris Messens +8 more
TL;DR: The active site proline in thioredoxin determines the driving potential for substrate reduction, and the oxidized form of wild-type Sa_Trx is far more stable than the reduced form over the whole temperature range.