Affiliation:
1. Department of Life Science and Basic Science Institute for Cell Damage Control, Sogang University, Seoul 121-742, South Korea
Abstract
ABSTRACT
The photosynthetic growth of
Synechocystis
sp. strain PCC 6803 is hampered by exogenously added bacteriochlorophyllide
a
(Bchlide
a
) in a dose-dependent manner. The growth inhibition caused by Bchlide
a
, however, is relieved by an increased level of exogenously added chlorophyllide
a
(Chlide
a
). The results are explained by the competitive inhibition of chlorophyll synthase by Bchlide
a
, with inhibition constants (
K
I
s) of 0.3 mM and 1.14 mM in the presence of sufficient geranylgeranyl pyrophosphate (GGPP) and phytyl pyrophosphate (PPP), respectively. Surprisingly, the bacteriochlorophyll synthase of
Rhodobacter sphaeroides
is inhibited competitively by Chlide
a
, with
K
I
s of 0.54 mM and 0.77 mM in the presence of sufficient GGPP and PPP, respectively. Consistently, exogenously added Chlide
a
inhibits the metabolic conversion of exogenously added Bchlide
a
to bacteriochlorophyll
a
by an
R. sphaeroides bchFNB-bchZ
mutant that neither synthesizes nor metabolizes Chlide
a
. The metabolic inhibition by Chlide
a
, however, is relieved by the elevated level of Bchlide
a
. Thus, the chlorophyll synthase of
Synechocystis
sp. PCC 6803 and the bacteriochlorophyll synthase of
R. sphaeroides
, both of which perform ping-pong-type reactions, are inhibited by Bchlide
a
and Chlide
a
, respectively. Although neither inhibitor is catalyzed by the target enzyme, inhibitions in the competitive mode suggest a structural similarity between their active sites.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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