Literature DB >> 10965946

Purification and properties of protoporphyrinogen oxidase from spinach chloroplasts.

N Watanabe1, F S Che, K Terashima, S Takayama, S Yoshida, A Isogai.   

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.

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Year:  2000        PMID: 10965946     DOI: 10.1093/pcp/pcd007

Source DB:  PubMed          Journal:  Plant Cell Physiol        ISSN: 0032-0781            Impact factor:   4.927


  3 in total

1.  Molecular characterization and subcellular localization of protoporphyrinogen oxidase in spinach chloroplasts.

Authors:  F S Che; N Watanabe; M Iwano; H Inokuchi; S Takayama; S Yoshida; A Isogai
Journal:  Plant Physiol       Date:  2000-09       Impact factor: 8.340

2.  Heterologous expression and purification of recombinant human protoporphyrinogen oxidase IX: A comparative study.

Authors:  Zora Novakova; Daria Khuntsaria; Marketa Gresova; Jana Mikesova; Barbora Havlinova; Shivam Shukla; Lucie Kolarova; Katerina Vesela; Pavel Martasek; Cyril Barinka
Journal:  PLoS One       Date:  2021-11-18       Impact factor: 3.240

3.  Characterization of HemY-type protoporphyrinogen IX oxidase genes from cyanobacteria and their functioning in transgenic Arabidopsis.

Authors:  Joonseon Yoon; Yunjung Han; Young Ock Ahn; Myoung-Ki Hong; Soon-Kee Sung
Journal:  Plant Mol Biol       Date:  2019-10-16       Impact factor: 4.076

  3 in total

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