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Metal free structure of SynFtn
Structural highlights
FunctionQ0I9X8_SYNS3 Iron-storage protein.[RuleBase:RU361145] Publication Abstract from PubMedThe gene encoding the cyanobacterial ferritin SynFtn is up-regulated in response to copper stress. Here, we show that, while SynFtn does not interact directly with copper, it is highly unusual in several ways. First, its catalytic diiron ferroxidase center is unlike those of all other characterized prokaryotic ferritins and instead resembles an animal H-chain ferritin center. Second, as demonstrated by kinetic, spectroscopic, and high-resolution X-ray crystallographic data, reaction of O2 with the di-Fe(2+) center results in a direct, one-electron oxidation to a mixed-valent Fe(2+)/Fe(3+) form. Iron-O2 chemistry of this type is currently unknown among the growing family of proteins that bind a diiron site within a four alpha-helical bundle in general and ferritins in particular. The mixed-valent form, which slowly oxidized to the more usual di-Fe(3+) form, is an intermediate that is continually generated during mineralization. Peroxide, rather than superoxide, is shown to be the product of O2 reduction, implying that ferroxidase centers function in pairs via long-range electron transfer through the protein resulting in reduction of O2 bound at only one of the centers. We show that electron transfer is mediated by the transient formation of a radical on Tyr40, which lies approximately 4 A from the diiron center. As well as demonstrating an expansion of the iron-O2 chemistry known to occur in nature, these data are also highly relevant to the question of whether all ferritins mineralize iron via a common mechanism, providing unequivocal proof that they do not. Reaction of O2 with a diiron protein generates a mixed-valent Fe(2+)/Fe(3+) center and peroxide.,Bradley JM, Svistunenko DA, Pullin J, Hill N, Stuart RK, Palenik B, Wilson MT, Hemmings AM, Moore GR, Le Brun NE Proc Natl Acad Sci U S A. 2019 Jan 18. pii: 1809913116. doi:, 10.1073/pnas.1809913116. PMID:30659147[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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