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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1074/jbc.m311869200

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
The Journal of biological chemistry
Volume:
279
Issue:
15
Pages:
15177-15182
Publication date:
2004-04-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:4df1485e-ec0e-42cd-af89-8dd45a68907f
Source identifiers:
32597
Local pid:
pubs:32597

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