Similarities and dissimilarities in the structure‐function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT‐IR difference spectroscopy

FEBS Letters

Hellwig, Petra²  Mäntele, Werner²  Buse, Gerhard¹  Soulimane, Tewfik¹ 

[1] Institut für Biochemie der Rheinisch-Westfälischen-Technischen Hochschule, Klinikum Aachen, Paulwelstr. 30, 52057 Aachen, Germany;Institut für Biophysik der Johann-Wolfgang-Goethe-Universität, Theodor-Stern-Kai 7, Haus 74, 60590 Frankfurt am Main, Germany

关键词: Bovine heart;    Cytochrome c oxidase;    UV-VIS spectroscopy;    FT-IR spectroscopy;    Protein electrochemistry;    Paracoccus denitrificans;   

DOI  :  10.1016/S0014-5793(99)01133-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The redox dependent changes in the cytochrome c oxidase from bovine heart were studied with a combined electrochemical and FT-IR spectroscopic approach. A direct comparison to the electrochemically induced FT-IR difference spectra of the cytochrome c oxidase from Paracoccus denitrificans reveals differences in the structure and intensity of vibrational modes. These differences are partially attributed to interactions of subunits influencing the heme and protein modes. In the spectral regions characteristic for ν(C=O) and ν(COO⁻)^s/as modes of protonated and deprotonated Asp and Glu residues, additional signals at 1736, 1602 and 1588 cm⁻¹ are observed. On this basis, the possible involvement of Asp-51, a residue specifically conserved in mammalian oxidase and previously proposed to show redox depended conformational changes in the respective X-ray structures, is critically discussed.

【 授权许可】

Unknown