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Néstor Carrillo
Researcher at National University of Rosario
Publications - 112
Citations - 4355
Néstor Carrillo is an academic researcher from National University of Rosario. The author has contributed to research in topics: Ferredoxin & Flavodoxin. The author has an hindex of 35, co-authored 107 publications receiving 3856 citations. Previous affiliations of Néstor Carrillo include National University of Cordoba & National Scientific and Technical Research Council.
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Open questions in ferredoxin‐NADP+ reductase catalytic mechanism
TL;DR: Using the formalism of the Albery-Knowles theory, which identifies which parameter(s) have to be modified to make these reductases even more proficient under a variety of conditions, natural or artificial, a rationale to interpret FNR evolution in terms of catalytic efficiency is provided.
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Generation of superoxide anion in chloroplasts of Arabidopsis thaliana during active photosynthesis: a focus on rapidly induced genes
TL;DR: The study suggests that genes involved in signalling pathways and with unknown functions are rapidly activated by superoxide anion generated in photosynthetically active chloroplasts, as part of the early antioxidant response of Arabidopsis leaves.
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A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.
Z. Deng,Alessandro Aliverti,Giuliana Zanetti,Adrián K. Arakaki,Jorgelina Ottado,Elena G. Orellano,Nora B. Calcaterra,Eduardo A. Ceccarelli,Néstor Carrillo,P.A. Karplus,P.A. Karplus +10 more
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.
reductase revealed by protein engineering and crystallographic studies
Z. Deng,Alessandro Aliverti,Giuliana Zanetti,Adrián K. Arakaki,Jorgelina Ottado,Nora B. Calcaterra,Eduardo A. Ceccarelli,Néstor Carrillo,P. Andrew Karplus +8 more
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.
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Plant-type ferredoxin-NADP+ reductases: a basal structural framework and a multiplicity of functions.
TL;DR: The aim of this article is to summarize information gained through recent developments, including the phyloge‐netic relationships among ferredoxin reductases and the key structural features of the plant FNR family.