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Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts
N Watanabe1, F S Che, K Terashima
1Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Japan.
Plant & Cell Physiology
|August 31, 2000
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.