Structural properties of 2/2 hemoglobins: The group III protein from Helicobacter hepaticus
| Autor: | David A. Vuletich, Matthew P. Pond, Benjamin Y. Winer, Henry J. Nothnagel, Juliette T. J. Lecomte |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular Protein Conformation Stereochemistry Molecular Sequence Data Clinical Biochemistry Biochemistry Article Ferrous Hemoglobins chemistry.chemical_compound Protein structure Genetics medicine Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Molecular Biology Heme Peptide sequence chemistry.chemical_classification Sequence Homology Amino Acid biology Cell Biology biology.organism_classification Amino acid NMR spectra database chemistry Ferric Helicobacter hepaticus medicine.drug |
| Zdroj: | IUBMB Life. 63:197-205 |
| ISSN: | 1521-6543 |
| DOI: | 10.1002/iub.430 |
| Popis: | The e-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 pKa 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 self-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 structure–function relationships. © 2011 IUBMB IUBMB Life, 63(3): 197–205, 2011 |
| Databáze: | OpenAIRE |
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