Biochemical and functional characterization of OsCSD3, a novel CuZn superoxide dismutase from rice.
作者： Ravi Prakash Sanyal , Amol Samant , Vishal Prashar , Hari Sharan Misra , Ajay Saini
DOI: 10.1042/BCJ20180516
关键词:
摘要: Superoxide dismutases (SODs, EC 1.15.1.1) belong to an important group of antioxidant metalloenzymes. Multiple SODs exist for scavenging reactive oxygen species (ROS) in different cellular compartments maintain intricate ROS balance. The present study deals with molecular and biochemical characterization CuZn SOD encoded by LOC_Os03g11960 (referred as OsCSD3), which is the least studied among four rice isozymes. OsCSD3 showed higher similarity peroxisomal plants. transcript was up-regulated response salinity, drought, oxidative stress. Full-length cDNA encoding cloned expressed Escherichia coli analyzed spectral characteristics. UV (ultraviolet)–visible spectroscopic analysis evidences d–d transitions, while circular dichroism indicated high β-sheet content protein. existed homodimer (∼36 kDa) both Cu 2+ Zn metal cofactors substantially active over a wide pH range (7.0–10.8), optimum 9.0. enzyme sensitive diethyldithiocarbamate but insensitive sodium azide, are characteristics features SODs. also exhibited bicarbonate-dependent peroxidase activity. Unlike several other known SODs, tolerance hydrogen peroxide thermal inactivation. Heterologous overexpression enhanced E. sod double-knockout (Δ sodA ΔsodB ) mutant wild-type strain against methyl viologen-induced stress, indicating vivo function this enzyme. results show that locus encodes functional similar
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