NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.

Journal article

Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein (Tomlinson, E. J., and Ferguson, S. J. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 5156-5160). To understand the effects of this change on the structure and dynamics of the protein, hetero-nuclear (15)N-edited NMR techniques have been used to characterize this b-type variant. The backbone (15)N, (1)H(N...

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Authors: Wain, R; Redfield, C; Ferguson, S; Smith, L

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 279
• Issue: 15
• Pages: 15177-15182
• Publication date: 2004-04-01
• DOI: 10.1074/jbc.m311869200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Protons; Molecular Sequence Data; Models, Molecular; Alanine; Protein Conformation; Hydrogen-Ion Concentration; Methionine; Bacteria, Aerobic; Mutagenesis; Cysteine; Heme; Hydrogen; Protein Structure, Secondary; Temperature; Protein Structure, Tertiary; Magnetic Resonance Spectroscopy; Amino Acid Sequence; Cytochrome c Group