ArticleJournal of molecular biology2010
High-resolution structure of the nitrile reductase QueF combined with molecular simulations provide insight into enzyme mechanism.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Unexpected NADPH Hydratase Activity in the Nitrile Reductase QueF from Escherichia coli.Chembiochem : a European journal of chemical biology · 2020Article
- Evidence of a sequestered imine intermediate during reduction of nitrile to amine by the nitrile reductase QueF fromThe Journal of biological chemistry · 2018Article
- Deazaguanine derivatives, examples of crosstalk between RNA and DNA modification pathways.RNA biology · 2017Review
- Protection of the Queuosine Biosynthesis Enzyme QueF from Irreversible Oxidation by a Conserved Intramolecular Disulfide.Biomolecules · 2017Article
- Crystal structure of the archaeosine synthase QueF-like-Insights into amidino transfer and tRNA recognition by the tunnel fold.Proteins · 2017Article
- Kinetic Analysis and Probing with Substrate Analogues of the Reaction Pathway of the Nitrile Reductase QueF from Escherichia coli.The Journal of biological chemistry · 2016Article
- Role of T cells in a gp91phox knockout murine model of acute allergic asthma.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2013Article
- Molecular modeling of the reaction pathway and hydride transfer reactions of HMG-CoA reductase.Biochemistry · 2012Article
- Structural basis of biological nitrile reduction.The Journal of biological chemistry · 2012Article
- Biosynthesis of pyrrolopyrimidines.Bioorganic chemistry · 2012Review
- Diversity of archaeosine synthesis in crenarchaeota.ACS chemical biology · 2012Article
- Defining the molecular role of gp91phox in the immune manifestation of acute allergic asthma using a preclinical murine model.Clinical and molecular allergy : CMA · 2012Article
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6 authors.
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Abstract
Here, we report the 1.53-Å crystal structure of the enzyme 7-cyano-7-deazaguanine reductase (QueF) from Vibrio cholerae, which is responsible for the complete reduction of a nitrile (CN) bond to a primary amine (H(2)C-NH(2)). At present, this is the only example of a biological pathway that includes reduction of a nitrile bond, establishing QueF as particularly noteworthy. The structure of the QueF monomer resembles two connected ferrodoxin-like domains that assemble into dimers. Ligands identified in the crystal structure suggest the likely binding conformation of the native substrates NADPH and 7-cyano-7-deazaguanine. We also report on a series of numerical simulations that have shed light on the mechanism by which this enzyme affects the transfer of four protons (and electrons) to the 7-cyano-7-deazaguanine substrate. In particular, the simulations suggest that the initial step of the catalytic process is the formation of a covalent adduct with the residue Cys194, in agreement with previous studies. The crystal structure also suggests that two conserved residues (His233 and Asp102) play an important role in the delivery of a fourth proton to the substrate.
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