In photosynthetically grown Rhodobacter capsulatus; heme is a qualitat
ively minor end product of the common tetrapyrrole pathway, but it may
play a significant regulatory role, Heme is synthesized from protopor
phyrin by the product of the hemH gene, ferrochelatase. We have cloned
the R. capsulatus hemH gene by complementation of an Escherichia coli
hemH mutant, When a plasmid carrying the hemH gene is returned to R,
capsulatus, ferrochelatase activity increases, aminolevulinate synthas
e activity decreases, and bacteriochlorophyll levels are dramatically
lowered. This is the first in vivo evidence to suggest that heme feedb
ack inhibits aminolevulinate synthase in R. capsulatus, thereby reduci
ng porphyrin synthesis.