- Abstract:
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© 2015 The Author(s). Cytochrome c
Expand abstract552 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 ... - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
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(pdf, 1.0MB)
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- Publisher copy:
- 10.1007/s10858-015-9938-3
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- 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:
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1573-5001
- ISSN:
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0925-2738
- URN:
-
uuid:c8138965-f1fd-4c44-b0e7-7dc1f635087e
- Source identifiers:
-
527989
- Local pid:
- pubs:527989
- Copyright holder:
- Tozawa et al.
- Copyright date:
- 2015
- Notes:
- © The Author(s) 2015. This article is published with open access at Springerlink.com. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License. This is the publisher's version of the article. The final version is available online from Springer Verlag at: [10.1007/s10858-015-9938-3]
Journal article
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b-type variant
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