An ionizable active-site tryptophan imparts catalase activity to a peroxidase core

Peter C. Loewen, Xavi Carpena, Pietro Vidossich, Ignacio Fita, Carme Rovira

Research output: Contribution to journalArticleResearchpeer-review

22 Citations (Scopus)

Abstract

Catalase peroxidases (KatGs) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatGs involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp. © 2014 American Chemical Society.
Original languageEnglish
Pages (from-to)7249-7252
JournalJournal of the American Chemical Society
Volume136
Issue number20
DOIs
Publication statusPublished - 21 May 2014

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