Current understanding of the function of magnesium chelatase.
Despite the global significance of chlorophylls and other modified tetrapyrroles, many aspects of their biosynthetic pathways are poorly understood. A key enzyme at the branch point between the haem and chlorophyll pathways, magnesium chelatase, couples the free energy of ATP hydrolysis to the insertion of magnesium into porphyrin, a process that is likely to be mediated through protein conformational changes. Conclusions from recent structural and functional studies of individual subunits are combined to provide a mechanistic outline of the full magnesium chelatase complex. Gathering further information presents a considerable challenge, and recent steps towards this goal will be introduced.
Reid
J D
JD
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. J.Reid@sheffield.ac.uk
Hunter
C N
CN
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D000458:Cyanobacteria / Q000201:enzymology; D007700:Kinetics; D008190:Lyases / Q000737:chemistry / Q000378:metabolism*; D011166:Porphyrins / Q000378:metabolism; D021122:Protein Subunits / Q000378:metabolism
D011166:Porphyrins; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D008190:Lyases; C086788:magnesium chelatase