Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin

Aik Hong Teh, Jennifer A. Saito, Aida Baharuddin, Jason R. Tuckerman, James S. Newhouse, Masaomi Kanbe, Elizabeth I. Newhouse, Rashidah Abdul Rahim, Frédérique Favier, Claude Didierjean, Eduardo H S Sousa, Matthew B. Stott, Peter F. Dunfield, Gonzalo Gonzalez, Marie Alda Gilles-Gonzalez, Nazalan Najimudin, Maqsudul Alam

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)3250-3258
Number of pages9
JournalFEBS Letters
Issue number20
StatePublished - Oct 20 2011


  • Crystal structure
  • Globin
  • Hell's Gate globin I
  • Molecular dynamics
  • Oxidation resistance
  • Oxygen binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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