Influence of amino acid side chain packing on Fe-methionine coordination in thermostable cytochrome C.
J Am Chem Soc
; 124(39): 11574-5, 2002 Oct 02.
Article
em En
| MEDLINE
| ID: mdl-12296704
ABSTRACT
Paramagnetic NMR and optical studies of the oxidized forms of mesophile Pseudomonas aeruginosa cytochrome c(551) and its quintuple mutant (F7A/V13M/F34Y/E43Y/V78I), and thermophile Hydrogenobacter thermophilus cytochrome c(552) demonstrated that the amino acid side chain packings in the protein interior influence the coordination bond between the heme iron and the axial methionine in the proteins. The strength of heme axial coordinations was found to correlate with the overall protein thermostability.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Grupo dos Citocromos c
/
Ferro
/
Metionina
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article