Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases

Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants.

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Main Authors: Ramana Gopavajhula,V., Viswanatha Chaitanya,K., Akbar Ali Khan,P., Shaik,Jilani P., Narasimha Reddy,P., Alanazi,Mohammad
Format: Digital revista
Language:English
Published: Sociedade Brasileira de Genética 2013
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000200013
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spelling oai:scielo:S1415-475720130002000132013-12-10Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutasesRamana Gopavajhula,V.Viswanatha Chaitanya,K.Akbar Ali Khan,P.Shaik,Jilani P.Narasimha Reddy,P.Alanazi,Mohammad amino acid analysis model evaluation molecular modeling phylogenetic analysis superoxide dismutase (SOD) Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants.info:eu-repo/semantics/openAccessSociedade Brasileira de GenéticaGenetics and Molecular Biology v.36 n.2 20132013-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000200013en10.1590/S1415-47572013005000023
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country Brasil
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libraryname SciELO
language English
format Digital
author Ramana Gopavajhula,V.
Viswanatha Chaitanya,K.
Akbar Ali Khan,P.
Shaik,Jilani P.
Narasimha Reddy,P.
Alanazi,Mohammad
spellingShingle Ramana Gopavajhula,V.
Viswanatha Chaitanya,K.
Akbar Ali Khan,P.
Shaik,Jilani P.
Narasimha Reddy,P.
Alanazi,Mohammad
Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
author_facet Ramana Gopavajhula,V.
Viswanatha Chaitanya,K.
Akbar Ali Khan,P.
Shaik,Jilani P.
Narasimha Reddy,P.
Alanazi,Mohammad
author_sort Ramana Gopavajhula,V.
title Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
title_short Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
title_full Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
title_fullStr Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
title_full_unstemmed Modeling and analysis of soybean (Glycine max. L) Cu/Zn, Mn and Fe superoxide dismutases
title_sort modeling and analysis of soybean (glycine max. l) cu/zn, mn and fe superoxide dismutases
description Superoxide dismutase (SOD, EC 1.15.1.1) is an important metal-containing antioxidant enzyme that provides the first line of defense against toxic superoxide radicals by catalyzing their dismutation to oxygen and hydrogen peroxide. SOD is classified into four metalloprotein isoforms, namely, Cu/Zn SOD, Mn SOD, Ni SOD and Fe SOD. The structural models of soybean SOD isoforms have not yet been solved. In this study, we describe structural models for soybean Cu/Zn SOD, Mn SOD and Fe SOD and provide insights into the molecular function of this metal-binding enzyme in improving tolerance to oxidative stress in plants.
publisher Sociedade Brasileira de Genética
publishDate 2013
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572013000200013
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