| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871681 | FEBS Letters | 2011 | 9 Pages |
Abstract
⺠HGbI is a bacterial globin that resists oxidation and functions at extremely acidic pH. ⺠Heme-iron coordination of ferrous HGbI shifts from 5- to 6-coordinate with increasing pH. ⺠HGbI is structurally similar to mammalian neuroglobins. ⺠HGbI has strikingly greater flexibility in the GH loop and H-helix upon O2 binding. ⺠Flexibility of Tyr29(B10) and rotation of Gln50(E7) may modulate ligand binding.
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Authors
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,