Molecular relaxation and metalloenzyme active site modeling

Metalloenzymes represent a broad class of important biomolecules containing an essential metal ion cofactor in their catalytic active sites, forming biologic metal complexes that perform a wide range of important functions: activation of small molecules (O2, N2, H2, CO), atom transfer chemistry, and...

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Autores principales: Scherlis, D.A., Martí, M.A., Ordejón, P., Estrin, D.A.
Formato: JOUR
Materias:
Active site modeling
Galactose oxidase
Manganese superoxide dismutase
Metalloenzymes
Molecular relaxation
Catalysis
Crystal structure
Molecular structure
Oxidation
Enzymes
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1529_Scherlis
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00207608_v90_n4-5_p1529_Scherlis
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spelling todo:paper_00207608_v90_n4-5_p1529_Scherlis2023-10-03T14:19:37Z Molecular relaxation and metalloenzyme active site modeling Scherlis, D.A. Martí, M.A. Ordejón, P. Estrin, D.A. Active site modeling Galactose oxidase Manganese superoxide dismutase Metalloenzymes Molecular relaxation Catalysis Crystal structure Molecular structure Oxidation Metalloenzymes Enzymes Metalloenzymes represent a broad class of important biomolecules containing an essential metal ion cofactor in their catalytic active sites, forming biologic metal complexes that perform a wide range of important functions: activation of small molecules (O2, N2, H2, CO), atom transfer chemistry, and the control of oxidation equivalents. The structures of many metalloenzyme active sites have been defined by X-ray crystallography, revealing transition metal ions in unique low-symmetry environments. These bioinorganic complexes present significant challenges for computational studies aimed at going beyond crystal structures to develop a detailed understanding of the catalytic mechanisms. Considerable progress has been made in the theoretical characterization of these sites in recent years, supported by the availability of efficient computational tools, in particular density functional methods. However, the ultimate success of a theoretical model depends on a number of factors independent of the specific computational method used, including the quality of the initial structural data, the identification of important environmental perturbations and constraints, and experimental validation of theoretical predictions. We explore these issues in detail and illustrate the effects of molecular relaxation in calculations of two metalloenzymes, manganese superoxide dismutase and galactose oxidase. © 2002 Wiley Periodicals, Inc. Int. J. Quantum Chem. 90. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1529_Scherlis
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Active site modeling
Galactose oxidase
Manganese superoxide dismutase
Metalloenzymes
Molecular relaxation
Catalysis
Crystal structure
Molecular structure
Oxidation
Metalloenzymes
Enzymes
spellingShingle Active site modeling
Galactose oxidase
Manganese superoxide dismutase
Metalloenzymes
Molecular relaxation
Catalysis
Crystal structure
Molecular structure
Oxidation
Metalloenzymes
Enzymes
Scherlis, D.A.
Martí, M.A.
Ordejón, P.
Estrin, D.A.
Molecular relaxation and metalloenzyme active site modeling
topic_facet Active site modeling
Galactose oxidase
Manganese superoxide dismutase
Metalloenzymes
Molecular relaxation
Catalysis
Crystal structure
Molecular structure
Oxidation
Metalloenzymes
Enzymes
description Metalloenzymes represent a broad class of important biomolecules containing an essential metal ion cofactor in their catalytic active sites, forming biologic metal complexes that perform a wide range of important functions: activation of small molecules (O2, N2, H2, CO), atom transfer chemistry, and the control of oxidation equivalents. The structures of many metalloenzyme active sites have been defined by X-ray crystallography, revealing transition metal ions in unique low-symmetry environments. These bioinorganic complexes present significant challenges for computational studies aimed at going beyond crystal structures to develop a detailed understanding of the catalytic mechanisms. Considerable progress has been made in the theoretical characterization of these sites in recent years, supported by the availability of efficient computational tools, in particular density functional methods. However, the ultimate success of a theoretical model depends on a number of factors independent of the specific computational method used, including the quality of the initial structural data, the identification of important environmental perturbations and constraints, and experimental validation of theoretical predictions. We explore these issues in detail and illustrate the effects of molecular relaxation in calculations of two metalloenzymes, manganese superoxide dismutase and galactose oxidase. © 2002 Wiley Periodicals, Inc. Int. J. Quantum Chem. 90.
format JOUR
author Scherlis, D.A.
Martí, M.A.
Ordejón, P.
Estrin, D.A.
author_facet Scherlis, D.A.
Martí, M.A.
Ordejón, P.
Estrin, D.A.
author_sort Scherlis, D.A.
title Molecular relaxation and metalloenzyme active site modeling
title_short Molecular relaxation and metalloenzyme active site modeling
title_full Molecular relaxation and metalloenzyme active site modeling
title_fullStr Molecular relaxation and metalloenzyme active site modeling
title_full_unstemmed Molecular relaxation and metalloenzyme active site modeling
title_sort molecular relaxation and metalloenzyme active site modeling
url http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1529_Scherlis
work_keys_str_mv AT scherlisda molecularrelaxationandmetalloenzymeactivesitemodeling
AT martima molecularrelaxationandmetalloenzymeactivesitemodeling
AT ordejonp molecularrelaxationandmetalloenzymeactivesitemodeling
AT estrinda molecularrelaxationandmetalloenzymeactivesitemodeling
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