Journal Article

Purification and Properties of Protoporphyrinogen Oxidase from Spinach Chloroplasts

Naohide Watanabe, Fang-Sik Che, Kenji Terashima, Seiji Takayama, Shigeo Yoshida and Akira Isogai

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 7, pages 889-892
Published in print July 2000 | ISSN: 0032-0781
Published online July 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcd007
Purification and Properties of Protoporphyrinogen Oxidase from Spinach Chloroplasts

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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 Protox-inhibiting herbicide, S23142, specifically inhibited the purified Protox activity at an IC50 value of 1 nM.

Keywords: Key words: Chloroplast — Herbicide — Protoporphyrin IX — Protoporphyrinogen oxidase — Spinacia oleracea L.; Abbreviations: BSA, bovine serum albumin; DM, n-dodecyl-β-d-glucoside; PMSF, phenylmethylsulfonyl fluoride; Protogen, protoporphyrinogen IX; Proto IX, protoporphyrin IX; Protox, protoporphyrinogen oxidase (EC 1.3.3.4).

Journal Article.  2508 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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