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Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin
Author(s) -
Teh Aik-Hong,
Saito Jennifer A.,
Baharuddin Aida,
Tuckerman Jason R.,
Newhouse James S.,
Kanbe Masaomi,
Newhouse Elizabeth I.,
Rahim Rashidah Abdul,
Favier Frédérique,
Didierjean Claude,
Sousa Eduardo H.S.,
Stott Matthew B.,
Dunfield Peter F.,
Gonzalez Gonzalo,
Gilles-Gonzalez Marie-Alda,
Najimudin Nazalan,
Alam Maqsudul
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.09.002
Subject(s) - globin , neuroglobin , heme , biochemistry , hemoglobin , chemistry , obligate , protein structure , hemeprotein , biology , protein superfamily , biophysics , gene , enzyme , ecology
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 °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.