Flavine nucleotide nitrate reductase from broad bean leaves
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概要
- 論文の詳細を見る
Hydrosulfite-reduced FMN served as an electron donor for nitrate reductase purified from broad bean leaves. FMN was successfully replaced with BV. The flavine nucleotide nitrate reductase had its pH optima at about 7.8 with phosphate buffer and at about 7.4 with Tris-HCl buffer. The Km's for nitrate and FMN were 3.7×10^<-4>M and 3.7×10^<-5>M, respectively. NADH_2: nitrate reductase activity was completely inhibited by 0.1mM p-CMB, whereas FMNH_2: nitrate reductase activity was not. Inhibited activity was restored by the addition of cysteine. A sulfhydryl enzyme is involved in the NADH_2: nitrate reductase system but not in the FMNH_2: nitrate reductase system. NADH_2 and FMNH_2 probably feed electrons into the electron transport chain at different sites. The nitrate reductase preparation had an NADH_2-specific diaphorase activity which was almost completely inhibited by 0.1mM p-CMB. The NADH specific diaphorase may form the sulfhydryl enzyme which mediates electron transfer between NADH_2 and nitrate.
- 日本植物生理学会の論文
著者
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Oji Yoshikiyo
Laboratory Of Plant Nutrition Faculty Of Agriculture Kobe University
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IZAWA GORO
Laboratory of Plant Nutrition, Faculty of Agriculture, Kobe University
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Izawa Goro
Laboratory Of Plant Nutrition Faculty Of Agriculture Kobe University
関連論文
- Effects of univalent cations on the formation of nitrate reductase and nitrite reductase in rice seedlings
- Flavine nucleotide nitrate reductase from broad bean leaves