## Abstract Eight different 2,2โฒโbipyridine derivatives, __i.e__. 2, 5, 8, 10, 12, 13, 15, and 19 (__Schemes 1__ and __2__), were prepared to study the influence of the chelating groups on the luminescence properties of their Eu^III^ and Tb^III^ chelates. According to our luminescence results, 2,2โฒ
Structural properties of 2/2 hemoglobins: The group III protein from Helicobacter hepaticus
โ 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
- DOI
- 10.1002/iub.430
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โฆ Synopsis
Abstract
The ฮตโproteobacterium 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 selfโassociated 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 structureโfunction relationships. ยฉ 2011 IUBMB IUBMB Life, 63(3): 197โ205, 2011
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