ArticlePlant physiology2008
Naphthoquinone-dependent generation of superoxide radicals by quinone reductase isolated from the plasma membrane of soybean.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 50 citations in OpenAlex.
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- How do holoparasitic plants exploit vitamin K1?Plant signaling & behavior · 2021Article
- Plasma membrane phylloquinone biosynthesis in nonphotosynthetic parasitic plants.Plant physiology · 2021Article
- Involvement of the MetO/Msr System in TwoInternational journal of molecular sciences · 2020Article
- The Cryptic Plastid ofmSphere · 2020Article
- A Key Role for Apoplastic HPlant physiology · 2017Article
- Article
- NADPH Oxidase-Dependent Superoxide Production in Plant Reproductive Tissues.Frontiers in plant science · 2016Review
- A product of heme catabolism modulates bacterial function and survival.PLoS pathogens · 2013Article
- Apoplastic superoxide production and peroxidase activity by intact and excised axenically grown seedling roots of sunflower.Protoplasma · 2012Article
- The rolB gene suppresses reactive oxygen species in transformed plant cells through the sustained activation of antioxidant defense.Plant physiology · 2012Article
- Article
- Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme.Nature · 2010Article
- Auxin-responsive genes AIR12 code for a new family of plasma membrane b-type cytochromes specific to flowering plants.Plant physiology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using a tetrazolium-based assay, a NAD(P)H oxidoreductase was purified from plasma membranes prepared from soybean (Glycine max) hypocotyls. The enzyme, a tetramer of 85 kD, produces O2(.-) by a reaction that depended on menadione or several other 1,4-naphthoquinones, in apparent agreement with a classification as a one-electron-transferring flavoenzyme producing semiquinone radicals. However, the enzyme displayed catalytic and molecular properties of obligatory two-electron-transferring quinone reductases of the DT-diaphorase type, including insensitivity to inhibition by diphenyleneiodonium. This apparent discrepancy was clarified by investigating the pH-dependent reactivity of menadionehydroquinone toward O2 and identifying the protein by mass spectrometry and immunological techniques. The enzyme turned out to be a classical NAD(P)H:quinone-acceptor oxidoreductase (EC 1.6.5.2, formerly 1.6.99.2) that reduces menadione to menadionehydroquinone and subsequently undergoes autoxidation at pH > or = 6.5. Autoxidation involves the production of the semiquinone as an intermediate, creating the conditions for one-electron reduction of O2. The possible function of this enzyme in the generation of O2(.-) and H2O2 at the plasma membrane of plants in vivo is discussed.
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