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By Mellor J.W.

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Protoporphyrin IX was not absolutely required as it was bound to the H protein, but additional protoporphyrin IX yielded higher activity and deuteroporphyrin IX substituted for protoporphyrin IX as a substrate. i" The lag period could be overcome by preincubation of the I and D proteins with Mg-ATP prior to addition of H and protoporphyrin IX to initiate the assay. The R. sphaeroides I, D, and H proteins were also heterologously expressed in E. I" Most of the D protein was expressed as inclusion bodies which were solubilized in 6 M urea and purified by metal ion affinity chromatography.

Under physiological conditions the requirement may be more or less than this. 5 6 Willows and Hansson III. Assay, Purification, and Properties of Magnesium Chelatase Magnesium chelatase is now known to be a multicomponent enzyme in numerous organisms based on both molecular genetics and biochemical assays. Its activity depends on the formation of an activation complex between the I and D proteins. The formation of this complex is dependent on both protein concentration and ATP. 26-3o The activation complex then catalyzes magnesium insertion into porphyrin only when combined with the H protein, Mg-ATP, porphyrin, and Mg(II).

9. Photosynthetic Purple Bacteria. . . . . . . . . . . . . . . . . . . . . . . . B. Magnesium Chelatase Genes. . . . . . . . . . . . . . . . . . . . . . . . . .. 1. Bacterial Gene Structure and Arrangement . . . . . . . . . . . . . . . . . . . .. 2. Gene Structure and Location in Plants and Algae. . . . . . . . . . . . . . . . . .. C. Regulation of Gene Expression .

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