Download MendeleyUnusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp.
Tarricone, C., Galizzi, A., Coda, A., Ascenzi, P., Bolognesi, M.(1997) Structure 5: 497-507
- PubMed: 9115439
- DOI: https://doi.org/10.1016/s0969-2126(97)00206-2
- Primary Citation of Related Structures:
1VHB, 2VHB - PubMed Abstract:
The first hemoglobin identified in bacteria was isolated from Vitreoscilla stercoraria (VtHb) as a homodimeric species. The wild-type protein has been reported to display medium oxygen affinity and cooperative ligand-binding properties. Moreover, VtHb can support aerobic growth in Escherichia coli with impaired terminal oxidase function. This ability of VtHb to improve the growth properties of E. coli has important applications in fermentation technology, assisting the overexpression of recombinant proteins and antibiotics. Oxygen binding heme domains have been identified in chimeric proteins from bacteria and yeast, where they are covalently linked to FAD- and NAD(P)H-binding domains. We investigate here the fold, the distal heme site structure and the quaternary assembly of a bacterial hemoglobin which does not bear the typical flavohemoglobin domain organization.
Organizational Affiliation:
Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Abbiategrasso 207, 27100, Pavia, Italy.
