The Ubiquinol Binding Site of Cytochrome bo3 from Escherichia coli Accommodates Menaquinone and Stabilizes a Functional Menasemiquinone

Biochemistry ◽  
2019 ◽  
Vol 58 (45) ◽  
pp. 4559-4569 ◽  
Author(s):  
Ziqiao Ding ◽  
Chang Sun ◽  
Sophia M. Yi ◽  
Robert B. Gennis ◽  
Sergei A. Dikanov
1994 ◽  
Vol 269 (46) ◽  
pp. 28834-28838
Author(s):  
R Welter ◽  
L.Q. Gu ◽  
L Yu ◽  
C.A. Yu ◽  
J Rumbley ◽  
...  

2017 ◽  
Vol 1858 (5) ◽  
pp. 366-370 ◽  
Author(s):  
Sylvia K. Choi ◽  
Myat T. Lin ◽  
Hanlin Ouyang ◽  
Robert B. Gennis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Amer H. Asseri ◽  
Albert Godoy-Hernandez ◽  
Hojjat Ghasemi Goojani ◽  
Holger Lill ◽  
Junshi Sakamoto ◽  
...  

AbstractCardiolipin (CL) is a lipid that is found in the membranes of bacteria and the inner membranes of mitochondria. CL can increase the activity of integral membrane proteins, in particular components of respiratory pathways. We here report that CL activated detergent-solubilized cytochrome bd, a terminal oxidase from Escherichia coli. CL enhanced the oxygen consumption activity ~ twofold and decreased the apparent KM value for ubiquinol-1 as substrate from 95 µM to 35 µM. Activation by CL was also observed for cytochrome bd from two Gram-positive species, Geobacillus thermodenitrificans and Corynebacterium glutamicum, and for cytochrome bo3 from E. coli. Taken together, CL can enhance the activity of detergent-solubilized cytochrome bd and cytochrome bo3.


1994 ◽  
Vol 269 (28) ◽  
pp. 18315-18319
Author(s):  
O. Bischof ◽  
V. Kruft ◽  
B. Wittmann-Liebold

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