Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics

Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommo...

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Veröffentlicht in:Journal of the American Chemical Society 2016-09, Vol.138 (37), p.12021-12024
Hauptverfasser: Lee, Hyelee, Fischer, Marcus, Shoichet, Brian K, Liu, Shih-Yuan
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container_issue 37
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container_title Journal of the American Chemical Society
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creator Lee, Hyelee
Fischer, Marcus
Shoichet, Brian K
Liu, Shih-Yuan
description Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102O···HN hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine’s distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting.
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subjects Boron Compounds - chemistry
Calorimetry
Hydrogen Bonding
Models, Molecular
Molecular Structure
Muramidase - chemistry
Muramidase - metabolism
Thermodynamics
title Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics
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