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Oxygen binding to catalase-peroxidase

AuthorsVidossich, Pietro; Carpena, Xavi ; Loewen, Peter C.; Fita, Ignacio ; Rovira, Carme
KeywordsHeme enzymes
Density functional calculations
Car−Parrinello method
Issue Date2011
PublisherAmerican Chemical Society
CitationJournal of Physical Chemistry Letters 2(3): 196- 200 (2011)
AbstractBy means of quantum mechanics/molecular mechanics calculations, we show that binding of dioxygen to the FeIII enzyme catalase-peroxidase (KatG), responsible for activating the antitubercular drug isoniazid, is possible in the absence of an external reducing agent, thanks to the unique electronic properties of the active site Met-Tyr-Trp adduct. The calculations give support to recent experimental observations suggesting that KatG activates molecular oxygen and suggest that dioxygen activation may be achieved in other enzymes by inserting a residue with low ionization potential near the active site. © 2011 American Chemical Society.
Identifiersdoi: 10.1021/jz1015795
e-issn: 1948-7185
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