Five Glutamic Acid Residues in the C-Terminal Domain of the ChlD Subunit Play a Major Role in Conferring Mg2+ Cooperativity upon Magnesium Chelatase
Author:
Affiliation:
1. Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, U.K.
2. Department of Chemistry, The University of Sheffield, Sheffield S3 7HF, U.K.
Funder
Biotechnology and Biological Sciences Research Council
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01080
Reference18 articles.
1. Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli.
2. 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
3. Characterization of the Binding of Deuteroporphyrin IX to the Magnesium Chelatase H Subunit and Spectroscopic Properties of the Complex
4. Direct Measurement of Metal-Ion Chelation in the Active Site of the AAA+ ATPase Magnesium Chelatase
5. Structure of the Cyanobacterial Magnesium Chelatase H Subunit Determined by Single Particle Reconstruction and Small-angle X-ray Scattering
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