Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.
Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.
复制标题
DOI:
10.1016/j.bbabio.2018.05.018
复制
发表时间:
2018-09
期刊:
影响因子:
--
通讯作者:
Rich PR
中科院分区:
文献类型:
--
作者:
Maréchal A;Hartley AM;Warelow TP;Meunier B;Rich PR
Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736 cm−1 in bovine CcO and previously assigned to D51 is absent from yeast CcO and couldn't be restored by introduction of a D residue at the equivalent position of the yeast protein. Redox spectra of yeast CcO also show much smaller changes in the amide I region, which may relate to structural differences in the region around D51 and the subunit I/II interface. Redox-induced FTIR difference spectra of WT and mutant yeast CcO are presented. Functionally-relevant features are compared with other A1-type haem copper oxidases. On oxidoreduction, all show perturbations of bovine residue E242 Introduction of bovine D51 in yeast doesn't result in an additional IR redox band. On photolysis of the FR-CO form all show perturbations of E242 and water molecules
登录
查看更多内容
影响因子:
64.8
作者:
IWATA, S;OSTERMEIER, C;MICHEL, H
通讯作者:
MICHEL, H
影响因子:
2.9
作者:
Gorbikova, EA;Vuorilehto, K;Verkhovsky, MI
通讯作者:
Verkhovsky, MI
影响因子:
4.3
作者:
Marechal, Amandine;Meunier, Brigitte;Rich, Peter R.
通讯作者:
Rich, Peter R.
影响因子:
3.5
作者:
ARTZATBANOV, VY;KONSTANTINOV, AA;SKULACHEV, VP
通讯作者:
SKULACHEV, VP
DOI:
10.1073/pnas.94.17.9085
发表时间:
1997-08-19
影响因子:
11.1
作者:
Konstantinov, AA;Siletsky, S;Gennis, RB
通讯作者:
Gennis, RB