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Originally published In Press as doi:10.1074/jbc.M002904200 on May 12, 2000

J. Biol. Chem., Vol. 275, Issue 31, 23583-23588, August 4, 2000
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Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits
IN VITRO CONFIRMATION OF NITROGENASE-LIKE FEATURES OF A BACTERIOCHLOROPHYLL BIOSYNTHESIS ENZYME*

Yuichi FujitaDagger and Carl E. Bauer§

From the Department of Biology, Indiana University, Bloomington, Indiana 47405

Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. The light-independent (dark) form of protochlorophyllide reductase plays a key role in the ability of gymnosperms, algae, and photosynthetic bacteria to green (form chlorophyll) in the dark. Genetic and sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein subunits that exhibit significant sequence similarity to the three subunits of nitrogenase, which catalyzes the reductive formation of ammonia from dinitrogen. However, unlike the well characterized features of nitrogenase, there has been no previous biochemical characterization of dark protochlorophyllide reductase. In this study, we report the first reproducible demonstration of dark protochlorophyllide reductase activity from purified protein subunits that were isolated from the purple nonsulfur photosynthetic bacterium Rhodobacter capsulatus. Two of the three subunits (Bchl and BchN) were expressed in R. capsulatus as S tag fusion proteins that facilitated affinity purification. The third subunit (BchB) was co-purified with the BchN protein indicating that BchN and BchB proteins form a tight complex. Dark protochlorophyllide reductase activity was shown to be dependent on the presence of all three subunits, ATP, and the reductant dithionite. The similarity of dark protochlorophyllide reductase to nitrogenase is discussed.

* This work was supported by National Insitutes of Health Grant GM539040 (to C. E. B) and the Ministry of Education, Science, and Culture of Japan (to Y. F.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Permanent address: Inst. for Protein Research, Osaka University, Suita, Osaka 565-0781, Japan.

§ To whom correspondence should be addressed: Dept. of Biology, Jordan Hall, Indiana University, Bloomington, IN 47408. Tel.: 812-855-6595; Fax: 812-856-4178; E-mail: cbauer@bio.indiana.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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