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Background: Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis. Results: Mutations in the AAA + domain of the magnesium chelatase ChlD subunit reduce but do not abolish catalytic activity. Conclusion: ChlD is an allosteric regulator of magnesium chelatase. Significance: These observations reveal an essential role for the ChlD protein in the first committed stage in chlorophyll biosynthesis. Magnesium chelatase is an AAA + ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA + domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA + domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg 2+ and MgATP 2− binding.
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Adams et al. (2013) studied this question.
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