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The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.

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 In this variant the two cysteines that form covalent thioether linkages to the heme group have been replaced by alanine residues (C11A/C14A).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...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m107572200

Authors


Pertinhez, TA More by this author
Tomlinson, EJ More by this author
Dobson, CM More by this author
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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

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