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• W1994408865 abstract "Abstract Ab initio density functional theory (DFT) methods were used to investigate the structural features of the active site of the binuclear enzyme rat liver arginase. Special emphasis was placed on the crucial role of the second shell ligand interactions. These interactions were systematically studied by performing calculations on models of varying size. It was determined that a water molecule, and not hydroxide, is the bridging exogenous ligand. The carboxylate ligands facilitate the close approach of the Mn (II) ions by attenuating the metal–metal electrostatic repulsion. Of the two metals, Mn A was shown to carry a larger positive charge. Analysis of the electronic properties of the active site revealed that orbitals involving the terminal Asp234 residue, as well as the flexible μ‐1,1 bridging Asp232, lie at high energies, suggesting weaker coordination. This is reflected in certain structural variability present in our models and is also consistent with recent experimental findings. Finally, implications of our findings for the biological function of the enzyme are delineated. Proteins 2004. © 2003 Wiley‐Liss, Inc." @default.
• W1994408865 created "2016-06-24" @default.
• W1994408865 creator A5036415725 @default.
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• W1994408865 date "2003-12-19" @default.
• W1994408865 modified "2023-10-18" @default.
• W1994408865 title "First principles computational study of the active site of arginase" @default.
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• W1994408865 doi "https://doi.org/10.1002/prot.10572" @default.
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