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Volume 270,
Number 8,
Issue of February 24, 1995 pp. 3732-3740
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Altered
Monovinyl and Divinyl Protochlorophyllide Pools in bchJ Mutants of Rhodobacter capsulatus POSSIBLE MONOVINYL SUBSTRATE DISCRIMINATION OF
LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE
(Received for publication, August 22, 1994; and in revised form, November 23, 1994)
Jon Y.
Suzuki ,
Carl E.
Bauer
In land plants in particular, it has been well established that
chlorophyll intermediates, Mg-protoporphyrin, Mg-protoporphyrin
monomethylester, protochlorophyllide, and chlorophyllide occur as
monovinyl and divinyl forms. The pool of monovinyl and divinyl
intermediates differ according to species, age of tissue, and light
regime. In this study, we investigated the monovinyl and divinyl
characteristics of protochlorophyllide and chlorophyllide in the purple
non-sulfur photosynthetic eubacterium Rhodobactercapsulatus. Our results indicate that mutations in genes
known to completely block the reduction of protochlorophyllide to
chlorophyllide (such as bchN, bchB, and bchL mutants), accumulate a pool of monovinyl and divinyl forms of
protochlorophyllide just as observed in plants. However, we also
observed that directed insertion and deletion mutations in bchJ, a gene located in the photosynthesis gene cluster,
affected the ratio of monovinyl and divinyl protochlorophyllide.
Specifically, bchJ-disrupted strains accumulate reduced levels
of bacteriochlorophyll concomitant with the accumulation of divinyl
protochlorophyllide. Mutants of bchJ in combination with a
second mutation in bchL still produce a mixed pool of
monovinyl and divinyl protochlorophyllide; however, the ratio of
monovinyl to divinyl protochlorophyllide is skewed in favor of divinyl
protochlorophyllide. These results thus identify bchJ as the
first sequenced gene that affects the divinyl to monovinyl ratio of
photopigment intermediates in any photosynthetic organism. In addition,
the results of our study also suggest that light-independent
protochlorophyllide reductase is discriminatory for a monovinyl
substrate.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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