title: Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts.
abstract: 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.
authors.affiliation: Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Watanabe
authors.forename: F S
authors.initials: FS
authors.lastname: Che
authors.forename: K
authors.initials: K
authors.lastname: Terashima
authors.forename: S
authors.initials: S
authors.lastname: Takayama
authors.forename: S
authors.initials: S
authors.lastname: Yoshida
authors.forename: A
authors.initials: A
authors.lastname: Isogai
mesh_terms: D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D044925:Oxidoreductases Acting on CH-CH Group Donors; D050768:Protoporphyrinogen Oxidase; D018724:Spinacia oleracea / Q000201:enzymology*
chemical_list: D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; D050768:Protoporphyrinogen Oxidase