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Arabidopsis glutathione‐dependent formaldehyde dehydrogenase is an S ‐nitrosoglutathione reductase
Author(s) -
Sakamoto Atsushi,
Ueda Manami,
Morikawa Hiromichi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02414-6
Subject(s) - formaldehyde dehydrogenase , complementation , s nitrosoglutathione , glutathione , biochemistry , glutathione reductase , arabidopsis thaliana , arabidopsis , escherichia coli , chemistry , reductase , complementary dna , heterologous expression , nitrate reductase , microbiology and biotechnology , recombinant dna , mutant , biology , enzyme , glutathione peroxidase , gene
S –Nitrosoglutathione (GSNO), an adduct of nitric oxide (NO) with glutathione, is known as a biological NO reservoir. Heterologous expression in Escherichia coli of a cDNA encoding a glutathione‐dependent formaldehyde dehydrogenase of Arabidopsis thaliana showed that the recombinant protein reduces GSNO. The identity of the cDNA was further confirmed by functional complementation of the hypersensitivity to GSNO of a yeast mutant with impaired GSNO metabolism. This is the first demonstration of a plant GSNO reductase, suggesting that plants possess the enzymatic pathway that modulates the bioactivity and toxicity of NO.