2006
DOI: 10.1016/j.tplants.2006.09.007
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Response to Zemojtel et al: Plant nitric oxide synthase: back to square one

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Cited by 222 publications
(173 citation statements)
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“…3B). To further characterize the source of NO during Cd 2+ treatment, similar experiments were performed in the atnoa1 mutant impaired in the expression of the AtNOA1 gene encoding an enzyme initially thought to catalyze NO synthesis from L-Arg (Crawford et al, 2006;Moreau et al, 2008). The mutant atnoa1 was reported to be impaired in NO synthesis or accumulation in response to abscisic acid or lipopolysaccharide treatments (Guo et al, 2003;Zeidler et al, 2004).…”
Section: Resultsmentioning
confidence: 99%
“…3B). To further characterize the source of NO during Cd 2+ treatment, similar experiments were performed in the atnoa1 mutant impaired in the expression of the AtNOA1 gene encoding an enzyme initially thought to catalyze NO synthesis from L-Arg (Crawford et al, 2006;Moreau et al, 2008). The mutant atnoa1 was reported to be impaired in NO synthesis or accumulation in response to abscisic acid or lipopolysaccharide treatments (Guo et al, 2003;Zeidler et al, 2004).…”
Section: Resultsmentioning
confidence: 99%
“…For example, the accumulation of plastid-targeted enzymes of the methylerythritol pathway causing fosmidomycin resistance in a recently isolated nos1 allele named resistant to inhibition by fosmidomycin1 (rif1) was unaffected by treatment with an NO donor (Flores-Pé rez et al, 2008). These results and the failure to reproduce the published results on the detection of NOS activity of the recombinant NOS1 protein (Crawford et al, 2006;Zemojtel et al, 2006a;Moreau et al, 2008) and the absence of such activity in bacterial homologs (Sudhamsu et al, 2008) led to the conclusion that NOS1 is not a NOS. However, compelling data on the specific biological role of this protein (renamed NITRIC OXIDE ASSOCIATED PROTEIN1 [NOA1]) have only recently been available.…”
Section: First Leads In the Hunt For Plant Nos Enzymesmentioning
confidence: 86%
“…This enzyme catalyzes the oxygen-and NADPHdependent oxidation of l-arginine to l-citrulline and NO in a complex reaction requiring FAD, FMN, BH 4 , Ca 2+ , and CaM [12,14,17,18]. In plants, pharmacological, biochemical and physicochemical, and immunological evidence indicates the presence of NOS-like activity similar, to a certain extent, to mammalian NOS [12,14,17,18,[22][23][24], although no plant NOS similar to the mammalian one has been characterized [19][20][21]. It has been shown that NOS is localized in the cytoplasm, chloroplasts, mitochondria, peroxisomes, and nucleus in plant cells [14,22,24,44].…”
Section: Discussionmentioning
confidence: 99%
“…In plants, there are several potential sources of NO, including NOS-like enzyme, nitrate reductase (NR), and non-enzymatic sources [12,14,15,17]. Although no plant NOS similar to the mammalian one has been identified [19][20][21], several lines of evidence have demonstrated the presence of NOS-like activity in plant cells [12,14,17,18,[22][23][24]. The NOS activity in pea leaf peroxisomes has been biochemically characterized, which is strictly dependent on l-arginine, NADPH, tetrahydrobiopterin (BH 4 ), and CaM, and requires Ca 2+ [22].…”
Section: Introductionmentioning
confidence: 99%