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Plant and Cell Physiology, 2000, Vol. 41, No. 7 889-892
© 2000 Oxford University Press

Purification and Properties of Protoporphyrinogen Oxidase from Spinach Chloroplasts

Naohide Watanabe1,3, Fang-Sik Che1,3,4, Kenji Terashima1, Seiji Takayama1, Shigeo Yoshida 2 and Akira Isogai1

1 Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8915-5, Takayama Ikoma, Nara, 630-0101 Japan 2 The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako-shi, Saitama, 351-0198 Japan

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.

3 These authors contributed equally to this paper.

4 Corresponding author: E-mail, fsche@bs.aist-nara.ac.jp; Fax, +81-743-72-5459.


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N. Watanabe, F.-S. Che, M. Iwano, S. Takayama, S. Yoshida, and A. Isogai
Dual Targeting of Spinach Protoporphyrinogen Oxidase II to Mitochondria and Chloroplasts by Alternative Use of Two In-frame Initiation Codons
J. Biol. Chem., June 1, 2001; 276(23): 20474 - 20481.
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