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Plasmodium falciparum ferredoxin-NADP+ reductase (FNR) is a FAD-containing enzyme that, in addition to be a promising target of novel antimalarial drugs, represents an excellent model of plant-type FNRs. The cofactor specificity of FNRs depends on differences in both kcat and Km values for NADPH and NADH. Here, we report that deletion of the hydroxyl group of the conserved Y258 of P. falciparum FNR, which interacts with the 2′-phosphate group of NADPH, selectively decreased the kcat of the NADPH-dependent reaction by a factor of 2 to match that of the NADH-dependent one. Rapid-reaction kinetics, active-site titrations with NADP+, and anaerobic photoreduction experiments indicated that this effect may be the consequence of destabilization of the catalytically competent conformation of bound NADPH. Moreover, because the Y258F replacement increased the Km for NADPH 4-fold and decreased that for NADH 3-fold, it led to a drop in the ability of the enzyme to discriminate between the coenzymes from 70- to just 1...
| Authors: | Sara Baroni; Vittorio Pandini; Maria Antonietta Vanoni; Alessandro Aliverti | |
| Journal: | Biochemistry | |
| Year: | 2012 | |
| DOI: | 10.1021/bi300078p | |
| Publication date: | 08-05-2012 |
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