The bilin prosthetic groups of the phytochrome photoreceptors and the light
-harvesting phycobiliprotein antennae arise from the oxygen-dependent ring
opening of heme. Two ferredoxin-dependent enzymes contribute to this conver
sion: a heme oxygenase and a bilin reductase with discrete double-bond spec
ificity. Using a dual plasmid system, one expressing a truncated cyanobacte
rial apophytochrome 1, Cph1(N514), and the other expressing a two-gene oper
on consisting of a heme oxygenase and a bilin reductase, these studies esta
blish the feasibility of producing photoactive phytochromes in any heme-con
taining cell. Heterologous expression systems for phytochromes not only wil
l facilitate genetic analysis of their assembly, spectrophotometric activit
y, and biological function, but also might afford the means to regulate gen
e expression by light in nonplant cells.