High thermal stability and unique trimer formation of cytochrome c' from thermophilic Hydrogenophilus thermoluteolus.
Biosci Biotechnol Biochem
; 77(8): 1677-81, 2013.
Article
em En
| MEDLINE
| ID: mdl-23924718
ABSTRACT
Sequence analysis indicated that thermophilic Hydrogenophilus thermoluteolus cytochrome c' (PHCP) and its mesophilic homolog, Allochromatium vinosum cytochrome c' (AVCP), closely resemble each other in a phylogenetic tree of the cytochrome c' family, with 55% sequence identity. The denaturation temperature of PHCP was 87 °C, 35 °C higher than that of AVCP. Furthermore, PHCP exhibited a larger enthalpy change value during its thermal denaturation than AVCP. While AVCP was dimeric, as observed previously, PHCP was trimeric, and this was the first observation as a cytochrome c'. Dissociation of trimeric PHCP and its protein denaturation reversibly occurred at the same time in a two-state transition manner. Therefore, PHCP is enthalpically more stable than AVCP, perhaps due to its unique trimeric form, in addition to the lower number of Gly residues in its putative α-helical regions.
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Base de dados:
MEDLINE
Assunto principal:
Estabilidade Enzimática
/
Chromatiaceae
/
Hydrogenophilaceae
/
Citocromos c'
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article