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Lookup NU author(s): Dr Jon Marles-WrightORCiD
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The heme prosthetic group is vital to many cellular processes and is therefore widespread throughout organisms of different phylogenetic origin. Heme is used in proteins involved in cellular respiration, acts as a chemical mediator in ligand binding and signalling proteins, and is the key co-factor in many enzymes. Strikingly, there are over 20 different folding topologies of b-type heme proteins that are able to incorporate the same, chemically identical heme ligand. Comparisons of structures show that heme-protein interactions are generally diverse, though a degree of conservation exists at contacts with the pyrrole rings, the propionate groups and the proximal ligand. These interaction "hot spots" presumably define major determinants for binding heme and provide guidelines for the future design of novel heme proteins. © The Royal Society of Chemistry.
Author(s): Schneider S, Marles-Wright J, Sharp KH, Paoli M
Publication type: Review
Publication status: Published
Journal: Natural Product Reports
Year: 2007
Volume: 24
Issue: 3
Pages: 621-630
ISSN (print): 0265-0568
ISSN (electronic): 1460-4752
URL: http://dx.doi.org/10.1039/b604186h
DOI: 10.1039/b604186h
PubMed id: 17534534
