| Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site. | |
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MedLine Citation:
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PMID: 18279389 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ferredoxin (flavodoxin)-NADP(H) reductases (FNRs) are ubiquitous flavoenzymes that deliver NADPH or low-potential one-electron donors (ferredoxin, flavodoxin, adrenodoxin) to redox-based metabolic reactions in plastids, mitochondria and bacteria. Plastidic FNRs are quite efficient reductases. In contrast, FNRs from organisms possessing a heterotrophic metabolism or anoxygenic photosynthesis display turnover numbers 20- to 100-fold lower than those of their plastidic and cyanobacterial counterparts. Several structural features of these enzymes have yet to be explained. The residue Y308 in pea FNR is stacked nearly parallel to the re-face of the flavin and is highly conserved amongst members of the family. By computing the relative free energy for the lumiflavin-phenol pair at different angles with the relative position found for Y308 in pea FNR, it can be concluded that this amino acid is constrained against the isoalloxazine. This effect is probably caused by amino acids C266 and L268, which face the other side of this tyrosine. Simple and double FNR mutants of these amino acids were obtained and characterized. It was observed that a decrease or increase in the amino acid volume resulted in a decrease in the catalytic efficiency of the enzyme without altering the protein structure. Our results provide experimental evidence that the volume of these amino acids participates in the fine-tuning of the catalytic efficiency of the enzyme. |
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Authors:
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Matías A Musumeci; Adrián K Arakaki; Daniela V Rial; Daniela L Catalano-Dupuy; Eduardo A Ceccarelli |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-02-12 |
Journal Detail:
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Title: The FEBS journal Volume: 275 ISSN: 1742-464X ISO Abbreviation: FEBS J. Publication Date: 2008 Mar |
Date Detail:
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Created Date: 2008-03-05 Completed Date: 2008-05-07 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 101229646 Medline TA: FEBS J Country: England |
Other Details:
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Languages: eng Pagination: 1350-66 Citation Subset: IM |
Affiliation:
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Molecular Biology Division, Instituto de Biología Molecular y Celular de Rosario (IBR), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Argentina. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Substitution Amino Acids / chemistry, genetics Catalysis Catalytic Domain / genetics Crystallography, X-Ray Ferredoxin-NADP Reductase / chemistry*, genetics Flavin-Adenine Dinucleotide / analysis, chemistry Hot Temperature Kinetics Mutation Protein Conformation Protein Folding Protein Structure, Secondary |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 146-14-5/Flavin-Adenine Dinucleotide; EC 1.18.1.2/Ferredoxin-NADP Reductase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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