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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Martí, Marcelo Adrián, Estrin, Dario Ariel
Publicado:	2002
Materias:	Active site modeling Galactose oxidase Manganese superoxide dismutase Metalloenzymes Molecular relaxation Catalysis Crystal structure Molecular structure Oxidation Enzymes
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1529_Scherlis 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	paper:paper_00207608_v90_n4-5_p1529_Scherlis
record_format	dspace
spelling	paper:paper_00207608_v90_n4-5_p1529_Scherlis2023-06-08T14:41:46Z Molecular relaxation and metalloenzyme active site modeling Martí, Marcelo Adrián Estrin, Dario Ariel 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. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1529_Scherlis 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 Martí, Marcelo Adrián Estrin, Dario Ariel 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.
author	Martí, Marcelo Adrián Estrin, Dario Ariel
author_facet	Martí, Marcelo Adrián Estrin, Dario Ariel
author_sort	Martí, Marcelo Adrián
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
publishDate	2002
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1529_Scherlis http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1529_Scherlis
work_keys_str_mv	AT martimarceloadrian molecularrelaxationandmetalloenzymeactivesitemodeling AT estrindarioariel molecularrelaxationandmetalloenzymeactivesitemodeling
_version_	1768544255677038592

Molecular relaxation and metalloenzyme active site modeling

Ejemplares similares