Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts

Authors
Watanabe, N Che, FS Terashima, K Takayama, S Yoshida, S Isogai, A
Citation
N. Watanabe et al., Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts, PLANT CEL P, 41(7), 2000, pp. 889-892
Citations number
22
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
PLANT AND CELL PHYSIOLOGY
ISSN journal
00320781 → ACNP
Volume
41
Issue
7
Year of publication
2000
Pages
889 - 892
Database
ISI
SICI code
0032-0781(200007)41:7<889:PAPOPO>2.0.ZU;2-O
Abstract
Protoporphyrinogen oxidase (Protox), an enzyme that catalyzes the common st ep 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 additi on of FAD, suggesting that chloroplast Protox requires FAD as a cofactor, F urthermore, the Protox-inhibiting herbicide, S23142, specifically inhibited the purified Protox activity at an IC50 value of 1 nM.