E
Eduardo A. Ceccarelli
Researcher at National University of Rosario
Publications - 84
Citations - 4705
Eduardo A. Ceccarelli is an academic researcher from National University of Rosario. The author has contributed to research in topics: Ferredoxin—NADP(+) reductase & Ferredoxin. The author has an hindex of 28, co-authored 82 publications receiving 4039 citations. Previous affiliations of Eduardo A. Ceccarelli include National Scientific and Technical Research Council & University of California, San Diego.
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Journal ArticleDOI
Selectivity of modification when latent and activated forms of the chloroplast F1-ATPase are inactivated by 7-chloro-4-nitrobenzofurazan.
TL;DR: In double labeling experiments, two-dimensional isoelectric focusing in the presence of urea followed by polyacrylamide gel electrophoresis in the absence of sodium dodecyl sulfate indicates that 2-azido-ADP, covalently bound at the tight ADP binding site, and the tyrosine modified by [14C]Nbf-Cl are located in different beta subunits.
Journal ArticleDOI
Conformational requirements of a recombinant ferredoxin-nadp+ reductase precursor for efficient binding to and import into isolated chloroplasts
TL;DR: Comparison of Km and Kd values under various conditions indicated that the binding step of the translocation process is largely irreversible, favouring import and processing, and a denatured precursor obtained by incubation with urea was a better substrate for plastid import than the holoprotein.
Journal ArticleDOI
Structural Backgrounds for the Formation of a Catalytically Competent Complex with Nadp(H) During Hydride Transfer in Ferredoxin-Nadp(+) Reductases.
Ana Sánchez-Azqueta,Matías A. Musumeci,Marta Martínez-Júlvez,Eduardo A. Ceccarelli,Milagros Medina +4 more
TL;DR: The overall findings indicate that in FNR the volume of the residue at position 266 is essential to attain the catalytic architecture between the nicotinamide and isoalloxazine rings at the active site and, therefore, for an efficient HT process.
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Structural-Functional Characterization and Physiological Significance of Ferredoxin-NADP+ Reductase from Xanthomonas axonopodis pv. citri
María Laura Tondo,Matías A. Musumeci,María Laura Delprato,Eduardo A. Ceccarelli,Elena G. Orellano +4 more
TL;DR: The results suggest that Xac-FNR is involved in the oxidative stress response of Xanthomonas axonopodis pv.
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Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide.
TL;DR: It is found that pea FNR ferricyanide diaphorase activity was inhibited by Zn2+ (Ki 1.57 microM), suggesting that the interaction of FNRs with their proteinaceous electron partners may induce a conformational change in the reductase that alters or completely prevents the inhibitory effect.