Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts

التفاصيل البيبلوغرافية
العنوان: Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts
المؤلفون: Shigeo Yoshida, Naohide Watanabe, Akira Isogai, Kenji Terashima, Fang-Sik Che, Seiji Takayama
المصدر: Plantcell physiology. 41(7)
سنة النشر: 2000
مصطلحات موضوعية: Oxidoreductases Acting on CH-CH Group Donors, Physiology, Plant Science, Cofactor, chemistry.chemical_compound, Spinacia oleracea, Protoporphyrinogen Oxidase, Heme, chemistry.chemical_classification, biology, Protoporphyrin IX, food and beverages, Cell Biology, General Medicine, biology.organism_classification, Chloroplast, Enzyme, Biochemistry, chemistry, Chlorophyll, biology.protein, Chromatography, Gel, Spinach, Protoporphyrinogen oxidase, Electrophoresis, Polyacrylamide Gel, Oxidoreductases
الوصف: Protoporphyrinogen oxidase (Protox), an enzyme that catalyzes the common step of chlorophyll and heme biosynthetic pathways, was purified from spinach chloroplasts. The molecular weight of purified protein was estimated to be approximately 60,000 by SDS-PAGE. Protox activity was stimulated by addition of FAD, suggesting that chloroplast Protox requires FAD as a cofactor. Furthermore, the Protoxinhibiting herbicide, S23142, specifically inhibited the purified Protox activity at an IC 50 value of 1 nM.
تدمد: 0032-0781
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36615653d60f5bae3bd0bb4357a5d622Test
https://pubmed.ncbi.nlm.nih.gov/10965946Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....36615653d60f5bae3bd0bb4357a5d622
قاعدة البيانات: OpenAIRE