The active site of magnesium chelatase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Plant Science
Link
http://www.nature.com/articles/s41477-020-00806-9.pdf
Reference55 articles.
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2. Medlock, A., Swartz, L., Dailey, T. A., Dailey, H. A. & Lanzilotta, W. N. Substrate interactions with human ferrochelatase. Proc. Natl Acad. Sci. USA 104, 1789–1793 (2007).
3. Medlock, A. E., Carter, M., Dailey, T. A., Dailey, H. A. & Lanzilotta, W. N. Product release rather than chelation determines metal specificity for ferrochelatase. J. Mol. Biol. 393, 308–319 (2009).
4. Hoggins, M., Dailey, H. A., Hunter, C. N. & Reid, J. D. Direct measurement of metal ion chelation in the active site of human ferrochelatase. Biochemistry 46, 8121–8127 (2007).
5. Hofbauer, S., Helm, J., Obinger, C., Djinović-Carugo, K. & Furtmüller, P. G. Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase. FEBS J. https://doi.org/10.1111/febs.15164 (2020).
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