Showing papers by "Eduardo A. Ceccarelli published in 1999"
TL;DR: In this article, the authors used mutants of this residue (Tyr 308) of pea ferredoxin-NADP+ reductase (FNR) to obtain the structures of productive NADP+ and NADPH complexes.
Abstract: The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.
182 citations
01 Jan 1999
TL;DR: It is shown that nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain, and the structures of productive NADP+ and NADPH complexes are revealed.
160 citations
TL;DR: In this article, it has been shown that a conserved metal ligand set is able to bind either one of two metal equivalents, i.e., one or two Zn(II)s, which may help in positioning the substrate for the nucleophilic attack.
64 citations