In plants the enzyme coproporphyrinogen oxidase catalyzes the oxidativ
e decarboxylation of coproporphyrinogen III to protoporphyrinogen IX i
n the heme and chlorophyll biosynthesis pathway(s). We have isolated a
soybean coproporphyrinogen oxidase cDNA from a cDNA library and deter
mined the primary structure of the corresponding gene. The coproporphy
rinogen oxidase gene encodes a polypeptide with a predicted molecular
mass of 43 kDa. The derived amino acid sequence shows 50% similarity t
o the corresponding yeast amino acid sequence. The main difference is
an extension of 67 amino acids at the N-terminus of the soybean polype
ptide which may function as a transit peptide. A full-length coproporp
hyrinogen oxidase cDNA clone complements a yeast mutant deleted of the
coproporphyrinogen oxidase gene, thus demonstrating the function of t
he soybean protein, The soybean coproporphyrinogen oxidase gene is hig
hly expressed in nodules at the stage where several late nodulins incl
uding leghemoglobin appear. The coproporphyrinogen oxidase mRNA is als
o detectable in leaves but at a lower level than in nodules while no m
RNA is detectable in roots. The high level of coproporphyrinogen oxida
se mRNA in soybean nodules implies that the plant increases heme produ
ction in the nodules to meet the demand for additional heme required f
or hemoprotein formation.