- Abstract:
-
NMR techniques and 8-anilino-1-napthalenesulphonate (ANS) binding studies have been used to characterize the apo state of a variant of cytochrome c(552) from Hydrogenobacter thermophilus. In this variant the two cysteines that form covalent thioether linkages to the heme group have been replaced by alanine residues (C11A/C14A). CD studies show that the apo state contains approximately 14% helical secondary structure, and measurements of hydrodynamic radii using pulse field gradient NMR method...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.m107572200
-
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- Journal:
- The Journal of biological chemistry
- Volume:
- 276
- Issue:
- 49
- Pages:
- 45813-45817
- Publication date:
- 2001-12-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:9e81584a-c4c2-4919-acb4-dd0f48a7db76
- Source identifiers:
-
31955
- Local pid:
- pubs:31955
- Copyright date:
- 2001
Journal article
The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.
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