Reduction of the Pea Ferredoxin-NADP(H) Reductase Catalytic Efficiency by the Structuring of a Carboxyl-Terminal Artificial Metal Binding Site
Author:
Affiliation:
1. Molecular Biology Division, Instituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi061152v
Reference53 articles.
1. Open questions in ferredoxin-NADP+ reductase catalytic mechanism
2. Atomic Structure of Ferredoxin-NADP + Reductase: Prototype for a Structurally Novel Flavoenzyme Family
3. Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7 Å Resolution: Oxidized, Reduced and 2′-Phospho-5′-AMP Bound States
4. X-ray Structure of the Ferredoxin:NADP+Reductase from the CyanobacteriumAnabaenaPCC 7119 at 1.8 Å Resolution, and Crystallographic Studies of NADP+Binding at 2.25 Å Resolution
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1. A new catalytic mechanism of bacterial ferredoxin‐NADP + reductases due to a particular NADP + binding mode;Protein Science;2021-08-21
2. Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2014-10
3. Ferredoxin:NADP+oxidoreductase in junction with CdSe/ZnS quantum dots: characteristics of an enzymatically active nanohybrid;Journal of Physics: Condensed Matter;2013-04-24
4. Structural-Functional Characterization and Physiological Significance of Ferredoxin-NADP+ Reductase from Xanthomonas axonopodis pv. citri;PLoS ONE;2011-11-09
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