Crystal structure of the catalytic subunit of magnesium chelatase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Plant Science
Link
http://www.nature.com/articles/nplants2015125.pdf
Reference37 articles.
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3. Gibson, L. C. D., Willows, R. D., Kannangara, C. G., von Wettstein, D. & Hunter, C. N. Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitiution of activity by combining the products of the bchH, -I and -D genes expressed in Escherichia coli. Proc. Natl Acad. Sci. USA 92, 1941–1944 (1995).
4. Jensen, P. E., Gibson, L. C. D., Henningsen, K. W. & Hunter, C. N. Expression of the chlI, chlD, and chlH genes from the cyanobacterium Synechocystis PCC6803 in Escherichia coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity. J. Biol. Chem. 271, 16662–16667 (1996).
5. Reid, J. D. & Hunter, C. N. Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803. J. Biol. Chem. 279, 26893–26899 (2004).
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