Thermodynamic analysis of l-arginine and Nω-hydroxy-l-arginine binding to nitric oxide synthase

Zakariassen, Henrik; Cederkvist, F. Henning; Harbitz, Espen; Shimizu, Tôru; Lange, Reinhard; Mayer, Bernd; Gorren, Antonius C.F.; Andersson, Karin; Sørlie, Morten

doi:10.1016/j.bbapap.2008.02.016

Cited by 2 publications

(2 citation statements)

References 46 publications

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“…The heat capacity changes observed for the binding of His and Arg to LAOBP (Table ) are more negative than those observed for the rigid‐body binding of small molecules to proteins (~5 to −100 cal mol −1 K −1 ; García‐Hernández et al ., ; Zakariassen and Sørlie, ; Zakariassen et al ., ; Chu et al ., ). In contrast, the Δ Cp b values determined in this work, as well as the few values reported for PBPs in the literature, are large and negative: −376 and −436 cal mol −1 K −1 for the complexes of l ‐galactose and l ‐arabinose with the arabinose binding protein (Fukada et al ., ) and −207 cal mol −1 K −1 for the binding of maltose to the maltose binding protein (Thomson et al ., ).…”

Section: Discussionmentioning

confidence: 97%

On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium

Pulido

Silva

Téllez

et al. 2015

J of Molecular Recognition

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The rational designing of binding abilities in proteins requires an understanding of the relationship between structure and thermodynamics. However, our knowledge of the molecular origin of high-affinity binding of ligands to proteins is still limited; such is the case for l-lysine-l-arginine-l-ornithine periplasmic binding protein (LAOBP), a periplasmic binding protein from Salmonella typhimurium that binds to l-arginine, l-lysine, and l-ornithine with nanomolar affinity and to l-histidine with micromolar affinity. Structural studies indicate that ligand binding induces a large conformational change in LAOBP. In this work, we studied the thermodynamics of l-histidine and l-arginine binding to LAOBP by isothermal titration calorimetry. For both ligands, the affinity is enthalpically driven, with a binding ΔCp of ~-300 cal mol(-1) K(-1) , most of which arises from the burial of protein nonpolar surfaces that accompanies the conformational change. Osmotic stress measurements revealed that several water molecules become sequestered upon complex formation. In addition, LAOBP prefers positively charged ligands in their side chain. An energetic analysis shows that the protein acquires a thermodynamically equivalent state with both ligands. The 1000-fold higher affinity of LAOBP for l-arginine as compared with l-histidine is mainly of enthalpic origin and can be ascribed to the formation of an extra pair of hydrogen bonds. Periplasmic binding proteins have evolved diverse energetic strategies for ligand recognition. STM4351, another arginine binding protein from Salmonella, shows an entropy-driven micromolar affinity toward l-arginine. In contrast, our data show that LAOBP achieves nanomolar affinity for the same ligand through enthalpy optimization.

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Section: Discussionmentioning

confidence: 97%

On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium

Pulido

Silva

Téllez

et al. 2015

J of Molecular Recognition

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“…In 2008, we identified more than 500 articles after searching Web of Science, PubMed, SciDir and OVID databases using ‘isothermal AND titration AND calorimetry’ or ITC or ‘Isothermal Titration Calorimetry’ search terms. Following the format of previous annual surveys these have been classified into the following categories: References cited in the text and review articles 1–82. Protein–protein and protein–peptide interactions 83–222. Protein–small ligand or protein–drug interactions 223–321. Protein/peptide metal interactions 322–355. Protein/peptide nucleic acid interactions 356–387. Protein/peptide lipid interactions …”

Section: Introductionmentioning

confidence: 99%

Survey of the year 2008: applications of isothermal titration calorimetry

Falconer

Penkova

Jelesarov

et al. 2010

J of Molecular Recognition

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Isothermal titration calorimetry (ITC) is a fast, accurate and label-free method for measuring the thermodynamics and binding affinities of molecular associations in solution. Because the method will measure any reaction that results in a heat change, it is applicable to many different fields of research from biomolecular science, to drug design and materials engineering, and can be used to measure binding events between essentially any type of biological or chemical ligand. ITC is the only method that can directly measure binding energetics including Gibbs free energy, enthalpy, entropy and heat capacity changes. Not only binding thermodynamics but also catalytic reactions, conformational rearrangements, changes in protonation and molecular dissociations can be readily quantified by performing only a small number of ITC experiments. In this review, we highlight some of the particularly interesting reports from 2008 employing ITC, with a particular focus on protein interactions with other proteins, nucleic acids, lipids and drugs. As is tradition in these reviews we have not attempted a comprehensive analysis of all 500 papers using ITC, but emphasize those reports that particularly captured our interest and that included more thorough discussions we consider exemplify the power of the technique and might serve to inspire other users.

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Thermodynamic analysis of l-arginine and Nω-hydroxy-l-arginine binding to nitric oxide synthase

Cited by 2 publications

References 46 publications

On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium

On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium

Survey of the year 2008: applications of isothermal titration calorimetry

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