Abstract
Rhodobacter capsulatus strain AJB530 excretes large amounts of coproporphyrin into the culture supernatant. The coproporphyrin was precipitable with ammonium sulfate, suggesting that it was part of a macromolecular complex. Analysis of an ammonium sulfate fraction indicated that the coproporphyrin was bound to a 66-kDa protein with a pI' of 4.0. The same protein was found in the culture supernatant of the bch+ strain PAS100.

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