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Magnesium-protoporphyrin chelatase, the first enzyme unique to the (bacterio)chlorophyll-specific branch of the porphyrin biosynthetic pathway, catalyzes the insertion of Mg2+ into protoporphyrin IX. Three genes, designatedbchI ,-D , and-H , from the strictly anaerobic and obligately phototrophic green sulfur bacteriumChlorobium vibrioforme show a significant level of homology to the magnesium chelatase-encoding genesbchI ,-D , and-H andchlI ,-D , and-H ofRhodobacter sphaeroides andSynechocystis strain PCC6803, respectively. These three genes were expressed inEscherichia coli ; the subsequent purification of overproduced BchI and -H proteins on an Ni2+ -agarose affinity column and denaturation of insoluble BchD protein in 6 M urea were required for reconstitution of Mg-chelatase activity in vitro. This work therefore establishes that the magnesium chelatase ofC. vibrioforme is similar to the magnesium chelatases of the distantly related bacteriaR. sphaeroides andSynechocystis strain PCC6803 with respect to number of subunits and ATP requirement. In addition, reconstitution of an active heterologous magnesium chelatase enzyme complex was obtained by combining theC. vibrioforme BchI and -D proteins and theSynechocystis strain PCC6803 ChlH protein. Furthermore, two versions, with respect to the N-terminal start of thebchI gene product, were expressed inE. coli , yielding ca. 38- and ca. 42-kDa versions of the BchI protein, both of which proved to be active. Western blot analysis of these proteins indicated that two forms of BchI, corresponding to the 38- and the 42-kDa expressed proteins, are also present inC. vibrioforme .

journal of bacteriology

Reconstitution of an Active Magnesium Chelatase Enzyme Complex from the bchI , -D , and -H Gene Products of the Green Sulfur Bacterium Chlorobium vibrioforme Expressed in Escherichia coli