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Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b-type variant

Abstract:

© 2015 The Author(s). Cytochrome c 552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of the two cysteine residues by alanines (Tomlinson and Ferguson in Proc Natl Acad Sci USA 97:5156-5160, 2000a). To probe the significance of the ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1007/s10858-015-9938-3

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
Publisher:
Springer Verlag Publisher's website
Journal:
Journal of Biomolecular NMR Journal website
Volume:
62
Issue:
2
Pages:
221-231
Publication date:
2015-05-08
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:c8138965-f1fd-4c44-b0e7-7dc1f635087e
Source identifiers:
527989
Local pid:
pubs:527989

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