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Structural properties of 2/2 hemoglobins: The group III protein from Helicobacter hepaticus

โœ Scribed by Henry J. Nothnagel; Benjamin Y. Winer; David A. Vuletich; Matthew P. Pond; Juliette T. J. Lecomte


Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
766 KB
Volume
63
Category
Article
ISSN
1521-6543

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โœฆ Synopsis


Abstract

The ฮตโ€proteobacterium Helicobacter hepaticus (Hh) contains a gene coding for a hemoglobin (Hb). The protein belongs to the 2/2 Hb lineage and is representative of group III, a set of Hbs about which little is known. An expression and purification procedure was developed for Hh Hb. Electronic absorption and nuclear magnetic resonance (NMR) spectra were used to characterize ligation states of the ferric and ferrous protein. The p__K__~a~ of the acid/alkaline transition of ferric Hh Hb was 7.3, an unusually low value. NMR analysis of the cyanomet complex showed the orientation of the heme group to be reversed when compared with most group I and group II 2/2 Hbs. Ferrous Hh Hb formed a stable cyanide complex that yielded NMR spectra similar to those of the carbonmonoxy complex. All forms of Hh Hb were selfโ€associated at NMR concentrations. Comparison was made to the related Campylobacter jejuni 2/2 Hb (Ctb), and the amino acid conservation pattern of group III was reinspected to help in the generalization of structureโ€“function relationships. ยฉ 2011 IUBMB IUBMB Life, 63(3): 197โ€“205, 2011


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