Molecular Cloning and Biochemical Characterization of the Iron Superoxide Dismutase from the Cyanobacterium Nostoc punctiforme ATCC 29133 and Its Response to Methyl Viologen-Induced Oxidative Stress

2015 ◽  
Vol 57 (11-12) ◽  
pp. 1003-1009 ◽  
Author(s):  
Lakshmipyari Devi Moirangthem ◽  
Kalibulla Syed Ibrahim ◽  
Rebecca Vanlalsangi ◽  
Karin Stensjö ◽  
Peter Lindblad ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Molecular Cloning ◽  
Methyl Viologen ◽  
Biochemical Characterization ◽  
Nostoc Punctiforme ◽  
Iron Superoxide Dismutase

Molecular Cloning and Biochemical Characterization of Iron Superoxide Dismutase from Leishmania braziliensis

2018 ◽  
Vol 60 (8) ◽  
pp. 595-600
Author(s):  
Camila C. B. Brito ◽  
Fernando V. Maluf ◽  
Gustavo M. A. de Lima ◽  
Rafael V. C. Guido ◽  
Marcelo S. Castilho
Keyword(s):  
Superoxide Dismutase ◽  
Molecular Cloning ◽  
Biochemical Characterization ◽  
Leishmania Braziliensis ◽  
Iron Superoxide Dismutase

scholarly journals Arabidopsis iron superoxide dismutase 1 protects against methyl viologen-induced oxidative stress in a copper-dependent manner

2021 ◽  
Author(s):  
Pavol Melicher ◽  
Petr Dvořák ◽  
Yuliya Krasylenko ◽  
Alexey Shapiguzov ◽  
Jaakko Kangasjärvi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Methyl Viologen ◽  
Accumulation Rate ◽  
Growth Media ◽  
Dependent Manner ◽  
Superoxide Dismutase 1 ◽  
Iron Superoxide Dismutase ◽  
Antioxidative Function

AbstractIron superoxide dismutase 1 (FSD1) was recently characterized as a plastidial, cytoplasmic, and nuclear superoxide dismutase with osmoprotective and antioxidative functions. However, its role in oxidative stress tolerance is not well understood. Here, we characterized the role of FSD1 in response to methyl viologen (MV)-induced oxidative stress in Arabidopsis thaliana. The findings demonstrated that the antioxidative function of FSD1 depends on the availability of Cu2+ in growth media. Prolonged MV exposure led to a decreased accumulation rate of superoxide, higher levels of hydrogen peroxide production, and higher protein carbonylation in the fsd1 mutants and transgenic plants lacking a plastidial pool of FSD1, compared to the wild type. MV led to a rapid increase in FSD1 activity, followed by a decrease. Chloroplastic localization of FSD1 is necessary for these changes. Proteomic analysis showed that the sensitivity of the fsd1 mutants coincided with decreased abundance of ferredoxin and light PSII harvesting complex proteins, with altered levels of signaling proteins. Collectively, the study provides evidence for the conditional antioxidative function of FSD1 and its possible role in signaling.

Molecular cloning and biochemical characterization of a Cu,Zn-superoxide dismutase from Scedosporium apiospermum

2007 ◽  
Vol 9 (5) ◽  
pp. 558-565 ◽  
Author(s):  
Osana C. Lima ◽  
Gérald Larcher ◽  
Patrick Vandeputte ◽  
Anne Lebouil ◽  
Dominique Chabasse ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Molecular Cloning ◽  
Biochemical Characterization ◽  
Scedosporium Apiospermum

Molecular Cloning and Characterization of a cDNA for an Iron-Superoxide Dismutase in Rice (Oryza sativaL.)

1999 ◽  
Vol 63 (2) ◽  
pp. 302-308 ◽  
Author(s):  
Hironori KAMINAKA ◽  
Shigeto MORITA ◽  
Megumi TOKUMOTO ◽  
Hidefumi YOKOYAMA ◽  
Takehiro MASUMURA ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Molecular Cloning ◽  
Iron Superoxide Dismutase
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