MAGNESIUM-PROTOPORPHYRIN CHELATASE OF RHODOBACTER-SPHAEROIDES - RECONSTITUTION OF ACTIVITY BY COMBINING THE PRODUCTS OF THE BCHH, BCHI, ANDBCHD GENES EXPRESSED IN ESCHERICHIA-COLI
Lcd. Gibson et al., MAGNESIUM-PROTOPORPHYRIN CHELATASE OF RHODOBACTER-SPHAEROIDES - RECONSTITUTION OF ACTIVITY BY COMBINING THE PRODUCTS OF THE BCHH, BCHI, ANDBCHD GENES EXPRESSED IN ESCHERICHIA-COLI, Proceedings of the National Academy of Sciences of the United Statesof America, 92(6), 1995, pp. 1941-1944
Magnesium-protoporphyrin chelatase lies at the branch point of the hem
e and (bacterio)chlorophyll biosynthetic pathways. In this work, the p
hotosynthetic bacterium Rhodobacter sphaeroides has been used as a mod
el system for the study of this reaction. The bchH and the bchI and -D
genes from R. sphaeroides were expressed in Escherichia coli. When ce
ll-free extracts from strains expressing BchH, BchI, and BchD were com
bined, the mixture was able to catalyze the insertion of Mg into proto
porphyrin IX in an ATP-dependent manner. This was possible only when a
ll three genes were expressed. The bchH, -I, and -D gene products are
therefore assigned to the Mg chelatase step in bacteriochlorophyll bio
synthesis. The mechanism of the Mg chelation reaction acid the implica
tions for chlorophyll biosynthesis in plants are discussed.