A study of the stabilization of semiquinones by the Escherichia coli quinol oxidase cytochrome bd

1996 ◽  
Vol 24 (1) ◽  
pp. 131-132 ◽  
Author(s):  
S. F. Hastings ◽  
W. J. Ingledew
Keyword(s):  
Escherichia Coli ◽  
Quinol Oxidase ◽  
Cytochrome Bd

scholarly journals A factor produced by Escherichia coli K-12 inhibits the growth of E. coli mutants defective in the cytochrome bd quinol oxidase complex: enterochelin rediscovered

Microbiology ◽  
1998 ◽  
Vol 144 (12) ◽  
pp. 3297-3308 ◽  
Author(s):  
G. M. Cook ◽  
C. Loder ◽  
B. Soballe ◽  
G. P. Stafford ◽  
J. Membrillo-Hernandez ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Quinol Oxidase ◽  
E Coli ◽  
Cytochrome Bd ◽  
K 12

The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli

Biochemistry ◽  
1994 ◽  
Vol 33 (50) ◽  
pp. 15110-15115 ◽  
Author(s):  
Bruce C. Hill ◽  
John J. Hill ◽  
Robert B. Gennis
Keyword(s):  
Escherichia Coli ◽  
Carbon Monoxide ◽  
Room Temperature ◽  
Temperature Reaction ◽  
Quinol Oxidase ◽  
Cytochrome Bd

scholarly journals Cytochrome bd promotes Escherichia coli biofilm antibiotic tolerance by regulating accumulation of noxious chemicals

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Connor J. Beebout ◽  
Levy A. Sominsky ◽  
Allison R. Eberly ◽  
Gerald T. Van Horn ◽  
Maria Hadjifrangiskou
Keyword(s):  
Escherichia Coli ◽  
Quinol Oxidase ◽  
E Coli ◽  
Cytochrome Bd ◽  
External Agents ◽  
Specific Increase ◽  
Matrix Production ◽  
Noxious Chemicals ◽  
Biofilm Development ◽  
Outer Membrane Permeability

AbstractNutrient gradients in biofilms cause bacteria to organize into metabolically versatile communities capable of withstanding threats from external agents including bacteriophages, phagocytes, and antibiotics. We previously determined that oxygen availability spatially organizes respiration in uropathogenic Escherichia coli biofilms, and that the high-affinity respiratory quinol oxidase cytochrome bd is necessary for extracellular matrix production and biofilm development. In this study we investigate the physiologic consequences of cytochrome bd deficiency in biofilms and determine that loss of cytochrome bd induces a biofilm-specific increase in expression of general diffusion porins, leading to elevated outer membrane permeability. In addition, loss of cytochrome bd impedes the proton mediated efflux of noxious chemicals by diminishing respiratory flux. As a result, loss of cytochrome bd enhances cellular accumulation of noxious chemicals and increases biofilm susceptibility to antibiotics. These results identify an undescribed link between E. coli biofilm respiration and stress tolerance, while suggesting the possibility of inhibiting cytochrome bd as an antibiofilm therapeutic approach.

scholarly journals Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli.

1990 ◽  
Vol 265 (8) ◽  
pp. 4364-4368 ◽  
Author(s):  
J C Salerno ◽  
B Bolgiano ◽  
R K Poole ◽  
R B Gennis ◽  
W J Ingledew
Keyword(s):  
Escherichia Coli ◽  
Quinol Oxidase ◽  
Cytochrome Bo

scholarly journals Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo3 solubilized in dodecyl-maltoside

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Amer H. Asseri ◽  
Albert Godoy-Hernandez ◽  
Hojjat Ghasemi Goojani ◽  
Holger Lill ◽  
Junshi Sakamoto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Oxygen Consumption ◽  
Integral Membrane Proteins ◽  
Terminal Oxidase ◽  
Geobacillus Thermodenitrificans ◽  
E Coli ◽  
Cytochrome Bd ◽  
Cytochrome Bo3 ◽  
Dodecyl Maltoside ◽  
Consumption Activity

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.

scholarly journals In Escherichia coli Ammonia Inhibits Cytochrome bo3 But Activates Cytochrome bd-I

Antioxidants ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 13
Author(s):  
Elena Forte ◽  
Sergey A. Siletsky ◽  
Vitaliy B. Borisov
Keyword(s):  
Escherichia Coli ◽  
Molecular Mechanisms ◽  
Dissociation Constants ◽  
Reductase Activity ◽  
Ammonia Concentration ◽  
High Concentration ◽  
E Coli ◽  
Cytochrome Bd ◽  
Cytochrome Bo3 ◽  
Oxygen Reductase

Interaction of two redox enzymes of Escherichia coli, cytochrome bo3 and cytochrome bd-I, with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution respirometry and absorption spectroscopy. At pH 7.0, the oxygen reductase activity of none of the enzymes is affected by the ligand. At pH 8.3, cytochrome bo3 is inhibited by the ligand, with 40% maximum inhibition at 100 mM (NH4)2SO4. In contrast, the activity of cytochrome bd-I at pH 8.3 increases with increasing the ligand concentration, the largest increase (140%) is observed at 100 mM (NH4)2SO4. In both cases, the effector molecule is apparently not NH4+ but NH3. The ligand induces changes in absorption spectra of both oxidized cytochromes at pH 8.3. The magnitude of these changes increases as ammonia concentration is increased, yielding apparent dissociation constants Kdapp of 24.3 ± 2.7 mM (NH4)2SO4 (4.9 ± 0.5 mM NH3) for the Soret region in cytochrome bo3, and 35.9 ± 7.1 and 24.6 ± 12.4 mM (NH4)2SO4 (7.2 ± 1.4 and 4.9 ± 2.5 mM NH3) for the Soret and visible regions, respectively, in cytochrome bd-I. Consistently, addition of (NH4)2SO4 to cells of the E. coli mutant containing cytochrome bd-I as the only terminal oxidase at pH 8.3 accelerates the O2 consumption rate, the highest one (140%) being at 27 mM (NH4)2SO4. We discuss possible molecular mechanisms and physiological significance of modulation of the enzymatic activities by ammonia present at high concentration in the intestines, a niche occupied by E. coli.

Assignment and Functional Roles of the cyoABCDE Gene Products Required for the Escherichia coli bo -Type Quinol Oxidase

1997 ◽  
Vol 122 (2) ◽  
pp. 415-421 ◽  
Author(s):  
H. Nakamura ◽  
K. Saiki ◽  
T. Mogi ◽  
Y. Anraku
Keyword(s):  
Escherichia Coli ◽  
Gene Products ◽  
Quinol Oxidase ◽  
Functional Roles
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