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Publication Abstract from PubMed

Hell's Gate globin I (HGbI), a heme-containing protein structurally homologous to mammalian neuroglobins, has been identified from an acidophilic and thermophilic obligate methanotroph, Methylacidiphilum infernorum. HGbI has very high affinity for O(2) and shows barely detectable autoxidation in the pH range of 5.2-8.6 and temperature range of 25-50 degrees C. Examination of the heme pocket by X-ray crystallography and molecular dynamics showed that conformational movements of Tyr29(B10) and Gln50(E7), as well as structural flexibility of the GH loop and H-helix, may play a role in modulating its ligand binding behavior. Bacterial HGbI's unique resistance to the sort of extreme acidity that would extract heme from any other hemoglobin makes it an ideal candidate for comparative structure-function studies of the expanding globin superfamily.

Hell's Gate globin I: an acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin.,Teh AH, Saito JA, Baharuddin A, Tuckerman JR, Newhouse JS, Kanbe M, Newhouse EI, Rahim RA, Favier F, Didierjean C, Sousa EH, Stott MB, Dunfield PF, Gonzalez G, Gilles-Gonzalez MA, Najimudin N, Alam M FEBS Lett. 2011 Oct 20;585(20):3250-8. Epub 2011 Sep 9. PMID:21925500^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.