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Characterization of N-terminal amino group–heme ligation emerging upon guanidine hydrochloric acid induced unfolding of Hydrogenobacter thermophilus ferricytochrome c 552
- Source :
- JBIC Journal of Biological Inorganic Chemistry. 13:25-34
- Publication Year :
- 2007
- Publisher :
- Springer Science and Business Media LLC, 2007.
-
Abstract
- Nonnative heme coordination structures emerging upon guanidine hydrochloric acid (GdnHCl) induced unfolding of Hydrogenobacter thermophilus ferricytochrome c552 were characterized by means of paramagnetic NMR. The heme coordination structure possessing the N-terminal amino group of the peptide chain in place of axial Met (His-Nterm form) was determined in the presence of GdnHCl concentrations in excess of 1.5 M at neutral pH. The stability of the His-Nterm form at pH 7.0 was found to be comparable with that of the bis-His form which has been recognized as a major nonnative heme coordination structure in cytochrome c folding/unfolding. Consequently, in addition to the bis-His form, the His-Nterm form is a substantial intermediate which affects the pathway and kinetics of the folding/unfolding of cytochromes c, of which the N-terminal amino groups are not acetylated.
- Subjects :
- Protein Denaturation
Circular dichroism
Cytochrome
Peptide
Heme
Biochemistry
Inorganic Chemistry
chemistry.chemical_compound
Guanidine
Nuclear Magnetic Resonance, Biomolecular
chemistry.chemical_classification
Bacteria
biology
Circular Dichroism
Cytochrome c
Hydrogenobacter thermophilus
Cytochromes c
Hydrogen-Ion Concentration
biology.organism_classification
Crystallography
chemistry
biology.protein
Spectrophotometry, Ultraviolet
Protein folding
Acids
Subjects
Details
- ISSN :
- 14321327 and 09498257
- Volume :
- 13
- Database :
- OpenAIRE
- Journal :
- JBIC Journal of Biological Inorganic Chemistry
- Accession number :
- edsair.doi.dedup.....8837e1f1c973866e78b813593ecfbae3