Purification and Properties of Protoporphyrinogen Oxidase from Spinach Chloroplasts | Zendy

Naohide Watanabe | Zendy; FangSik Che | Zendy; Kenji Terashima | Zendy; Seiji Takayama | Zendy; Shigeo Yoshida | Zendy; Akira Isogai | Zendy

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Purification and Properties of Protoporphyrinogen Oxidase from Spinach Chloroplasts

Author(s) -

Naohide Watanabe,

FangSik Che,

Kenji Terashima,

Seiji Takayama,

Shigeo Yoshida,

Akira Isogai

Publication year - 2000

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcd007

Subject(s) - protoporphyrinogen oxidase , spinach , chloroplast , biochemistry , enzyme , chemistry , cofactor , gene

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.

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