Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.

Abstract:

:In order to elucidate the molecular mechanisms responsible for the apparent nonlinear behavior of the temperature dependence of the redox potential of Hydrogenobacter thermophilus cytochrome c552 [Takahashi, Y., Sasaki, H., Takayama, S. J., Mikami, S., Kawano, S., Mita, H., Sambongi, Y., and Yamamoto, Y. (2006) Biochemistry 45, 11005-11011], its heme active site structure has been characterized using variable-temperature and -pressure NMR techniques. The study revealed a temperature-dependent conformational transition between protein structures, which slightly differ in the conformation of the loop bearing the Fe-bound axial Met residue. The heme environment in the protein structure which arises at lower temperature was found to be more polar, as a result of the altered orientation of the loop with respect to the heme due to its conformational change, than that arising at higher temperature. The present study demonstrated the importance of the structural and dynamic properties of the polypeptide chain in close proximity to the heme for redox regulation of the protein.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Takayama SJ,Takahashi YT,Mikami S,Irie K,Kawano S,Yamamoto Y,Hemmi H,Kitahara R,Yokoyama S,Akasaka K

doi

10.1021/bi7000714

subject

Has Abstract

pub_date

2007-08-14 00:00:00

pages

9215-24

issue

32

eissn

0006-2960

issn

1520-4995

journal_volume

46

pub_type

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