First published online November 7, 2002; 10.1104/pp.008128
Plant Physiol, December 2002, Vol. 130, pp. 1958-1966
Expression and Biochemical Properties of a Ferredoxin-Dependent
Heme Oxygenase Required for Phytochrome Chromophore
Synthesis1
Takuya
Muramoto,2
Noriyuki
Tsurui,
Matthew J.
Terry,
Akiho
Yokota, and
Takayuki
Kohchi*
Graduate School of Biological Sciences, Nara Institute of Science
and Technology, Ikoma, Nara 630-0101, Japan (T.M., N.T., A.Y., T.K.);
and School of Biological Sciences, University of Southampton,
Southampton SO16 7PX, United Kingdom (M.J.T.)
The HY1 gene of Arabidopsis encodes a plastid
heme oxygenase (AtHO1) required for the synthesis of the chromophore of
the phytochrome family of plant photoreceptors. To determine the
enzymatic properties of plant heme oxygenases, we have expressed the
HY1 gene (without the plastid transit peptide) in
Escherichia coli to produce an amino terminal fusion
protein between AtHO1 and glutathione S-transferase. The
fusion protein was soluble and expressed at high levels. Purified
recombinant AtHO1, after glutathione S-transferase
cleavage, is a hemoprotein that forms a 1:1 complex with heme. In the
presence of reduced ferredoxin, AtHO1 catalyzed the formation of
biliverdin IX from heme with the concomitant production of carbon
monoxide. Heme oxygenase activity could also be reconstituted using
photoreduced ferredoxin generated through light irradiation of isolated
thylakoid membranes, suggesting that ferredoxin may be the electron
donor in vivo. In addition, AtHO1 required an iron chelator and second
reductant, such as ascorbate, for full activity. These results show
that the basic mechanism of heme cleavage has been conserved between
plants and other organisms even though the function, subcellular
localization, and cofactor requirements of heme oxygenases differ substantially.
1
This work was supported in part by the
"Research for the Future" Program 00L01605 from the Japan Society
for the Promotion of Science (to T.K.), by the Royal Society University
(Research Fellowship to M.J.T.), and by the UK Biotechnology and
Biological Sciences Research Council (grant nos. 51/P10948 and ISIS982
to M.J.T.).
2
Present address: Institute for Chemical Research, Kyoto
University, Uji, Kyoto 611-0011, Japan.
*
Corresponding author; e-mail kouchi{at}bs.aist-nara.ac.jp; fax
81-743-72-5569.
© 2002 American Society of Plant Biologists
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