Characterization of the magnesium chelatase from Thermosynechococcus elongatus
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.
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://portlandpress.com/biochemj/article-pdf/457/1/163/678724/bj4570163.pdf
Reference42 articles.
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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;Jensen;J. Biol. Chem.,1996
3. Human ferrochelatase: characterization of substrate-iron binding and proton-abstracting residues;Sellers;Biochemistry,2001
4. The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis;Wu;Nat. Struct. Biol.,2001
5. The cell biology of tetrapyrroles: a life and death struggle;Mochizuki;Trends Plant Sci.,2010
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