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

doi:10.1016/j.febslet.2011.09.002

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 journal › Article › peer-review

28 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	3250-3258
Number of pages	9
Journal	FEBS Letters
Volume	585
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2011.09.002
State	Published - Oct 20 2011

Keywords

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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10.1016/j.febslet.2011.09.002

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Teh, A. H., Saito, J. A., Baharuddin, A., Tuckerman, J. R., Newhouse, J. S., Kanbe, M., Newhouse, E. I., Rahim, R. A., Favier, F., Didierjean, C., Sousa, E. H. S., Stott, M. B., Dunfield, P. F., Gonzalez, G., Gilles-Gonzalez, M. A., Najimudin, N., & Alam, M. (2011). Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin. FEBS Letters, 585(20), 3250-3258. https://doi.org/10.1016/j.febslet.2011.09.002

Teh, AH, Saito, JA, Baharuddin, A, Tuckerman, JR, Newhouse, JS, Kanbe, M, Newhouse, EI, Rahim, RA, Favier, F, Didierjean, C, Sousa, EHS, Stott, MB, Dunfield, PF, Gonzalez, G, Gilles-Gonzalez, MA, Najimudin, N & Alam, M 2011, 'Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin', FEBS Letters, vol. 585, no. 20, pp. 3250-3258. https://doi.org/10.1016/j.febslet.2011.09.002

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

abstract = "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.",

keywords = "Crystal structure, Globin, Hell's Gate globin I, Molecular dynamics, Oxidation resistance, Oxygen binding",

author = "Teh, {Aik Hong} and Saito, {Jennifer A.} and Aida Baharuddin and Tuckerman, {Jason R.} and Newhouse, {James S.} and Masaomi Kanbe and Newhouse, {Elizabeth I.} and Rahim, {Rashidah Abdul} and Fr{\'e}d{\'e}rique Favier and Claude Didierjean and Sousa, {Eduardo H S} and Stott, {Matthew B.} and Dunfield, {Peter F.} and Gonzalo Gonzalez and Gilles-Gonzalez, {Marie Alda} and Nazalan Najimudin and Maqsudul Alam",

note = "Funding Information: This work was supported by the U.S. Army Telemedicine and Advanced Technology Research Center ( W81XWH0520013 ) to M.A., intramural funding from the Centre for Chemical Biology, Universiti Sains Malaysia (CCB@USM) , and U.S. National Science Foundation Grant No. MCB620531 (M.A.G.G.). The authors acknowledge the Tikitere Trust, the owners and guardians of Hell{\textquoteright}s Gate. ",

year = "2011",

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day = "20",

doi = "10.1016/j.febslet.2011.09.002",

language = "English (US)",

volume = "585",

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T1 - Hell's Gate globin I

T2 - An acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin

AU - Teh, Aik Hong

AU - Saito, Jennifer A.

AU - Baharuddin, Aida

AU - Tuckerman, Jason R.

AU - Newhouse, James S.

AU - Kanbe, Masaomi

AU - Newhouse, Elizabeth I.

AU - Rahim, Rashidah Abdul

AU - Favier, Frédérique

AU - Didierjean, Claude

AU - Sousa, Eduardo H S

AU - Stott, Matthew B.

AU - Dunfield, Peter F.

AU - Gonzalez, Gonzalo

AU - Gilles-Gonzalez, Marie Alda

AU - Najimudin, Nazalan

AU - Alam, Maqsudul

N1 - Funding Information: This work was supported by the U.S. Army Telemedicine and Advanced Technology Research Center ( W81XWH0520013 ) to M.A., intramural funding from the Centre for Chemical Biology, Universiti Sains Malaysia (CCB@USM) , and U.S. National Science Foundation Grant No. MCB620531 (M.A.G.G.). The authors acknowledge the Tikitere Trust, the owners and guardians of Hell’s Gate.

PY - 2011/10/20

Y1 - 2011/10/20

N2 - 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.

AB - 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.

KW - Crystal structure

KW - Globin

KW - Hell's Gate globin I

KW - Molecular dynamics

KW - Oxidation resistance

KW - Oxygen binding

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JO - FEBS Letters

JF - FEBS Letters

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ER -

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

Abstract

Keywords

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