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Article

Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum.

The Journal of biological chemistry - 3 Nov 2006

McMillan Paul J, Arscott L David, Ballou David P, Becker Katja, Williams Charles H, Müller Sylke

Abstract excerpt

High-M(r) thioredoxin reductase from the malaria parasite Plasmodium falciparum (PfTrxR) contains three redox active centers (FAD, Cys-88/Cys-93, and Cys-535/Cys-540) that are in redox communication. The catalytic mechanism of PfTrxR, which involves dithiol-disulfide interchanges requiring acid-base catalysis, was studied by steady-state kinetics, spectral analyses of anaerobic static titrations, and rapid...

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PMID: 16950793
DOI: 10.1074/jbc.M601141200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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