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Volume 271, Number 15, Issue of April 12, 1996 pp. 8714-8718
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Protoporphyrinogen Oxidase of Myxococcus xanthus
EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF THE CLONED ENZYME

(Received for publication, September 28, 1995; and in revised form, January 26, 1996)

Harry A. Dailey ,  Tamara A. Dailey

Protoporphyrinogen oxidase (EC 1.3.3.4) catalyzes the six electron oxidation of protoporphyrinogen IX to protoporphyrin IX. The enzyme from the bacterium Myxococcus xanthus has been cloned, expressed, purified, and characterized. The protein has been expressed in Escherichia coli using a Tac promoter-driven expression plasmid and purified to apparent homogeneity in a rapid procedure that yields approximately 10 mg of purified protein per liter of culture. Based upon the deduced amino acid sequence the molecular weight of a single subunit is 49,387. Gel permeation chromatography in the presence of 0.2% n-octyl-beta-D-glucopyranoside yields a molecular weight of approximately 100,000 while SDS gel electrophoresis shows a single band at 50,000. The native enzyme is, thus, a homodimer. The purified protein contains a non-covalently bound FAD but no detectable redox active metal. The M. xanthus enzyme utilizes protoporphyrinogen IX, but not coproporphyrinogen III, as substrate and produces 3 mol of H(2)O(2)/mol of protoporphyrin. The apparent K and k for protoporphyrinogen in assays under atmospheric concentrations of oxygen are 1.6 µM and 5.2 min, respectively. The diphenyl ether herbicide acifluorfen at 1 µM strongly inhibits the enzyme's activity.



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