Terminal Oxidase Cytochrome bd Protects Bacteria Against Hydrogen Sulfide Toxicity

2021 ◽  
Vol 86 (1) ◽  
pp. 22-32
Author(s):  
Vitaliy B. Borisov ◽  
Elena Forte
Keyword(s):  
Hydrogen Sulfide ◽  
Terminal Oxidase ◽  
Cytochrome Bd ◽  
Sulfide Toxicity

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.

Characterization of hydrogen sulfide toxicity to human corneal stromal fibroblasts

2020 ◽  
Vol 1480 (1) ◽  
pp. 207-218
Author(s):  
Praveen K. Balne ◽  
Nishant R. Sinha ◽  
Alexandria C. Hofmann ◽  
Lynn M. Martin ◽  
Rajiv R. Mohan
Keyword(s):  
Hydrogen Sulfide ◽  
Stromal Fibroblasts ◽  
Sulfide Toxicity

Cyanide-insensitive quinol oxidase (CIO) from Gluconobacter oxydans is a unique terminal oxidase subfamily of cytochrome bd

2013 ◽  
Vol 153 (6) ◽  
pp. 535-545 ◽  
Author(s):  
Hiroshi Miura ◽  
Tatsushi Mogi ◽  
Yoshitaka Ano ◽  
Catharina T. Migita ◽  
Minenosuke Matsutani ◽  
...  
Keyword(s):  
Gluconobacter Oxydans ◽  
Terminal Oxidase ◽  
Quinol Oxidase ◽  
Cytochrome Bd

scholarly journals How bacteria breathe in hydrogen sulfide-rich environments

2016 ◽  
Vol 38 (5) ◽  
pp. 8-11 ◽  
Author(s):  
Elena Forte ◽  
Alessandro Giuffrè
Keyword(s):  
Hydrogen Sulfide ◽  
Mitochondrial Respiratory Chain ◽  
Cell Respiration ◽  
Human Gut ◽  
Natural Habitats ◽  
Cytochrome Bd ◽  
Physiological Processes ◽  
Signalling Molecule ◽  
Potential Impact ◽  
High Concentrations

Hydrogen sulfide (H2S) is now universally recognized as an endogenous signalling molecule playing a central role in human physiology. This gas, although it controls a number of physiological processes at low (submicromolar) concentrations, is toxic at high concentrations as it blocks cell respiration by potently inhibiting cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain. In a recent study on the model micro-organism Escherichia coli, it was shown that the bacterial respiratory oxidase cytochrome bd is resistant to H2S inhibition, thus enabling bacterial O2 respiration and growth in the presence of sulfide. This may be relevant because many microbes are H2S producers and some of them live in sulfide-rich environments, such as the human gut and other natural habitats. The potential impact of this finding in different areas (environment, life evolution and human health) is discussed.

scholarly journals Terminal Oxidases of Bacillus subtilisStrain 168: One Quinol Oxidase, Cytochromeaa3 or Cytochrome bd, Is Required for Aerobic Growth

2000 ◽  
Vol 182 (23) ◽  
pp. 6557-6564 ◽  
Author(s):  
Lena Winstedt ◽  
Claes von Wachenfeldt
Keyword(s):  
Bacillus Subtilis ◽  
Sequence Analysis ◽  
Terminal Oxidase ◽  
Rich Medium ◽  
Aerobic Growth ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Cytochrome Bd ◽  
Heme Copper Oxidases ◽  
Quinol Oxidases

ABSTRACT The gram-positive endospore-forming bacterium Bacillus subtilis has, under aerobic conditions, a branched respiratory system comprising one quinol oxidase branch and one cytochrome oxidase branch. The system terminates in one of four alternative terminal oxidases. Cytochrome caa 3 is a cytochromec oxidase, whereas cytochrome bd and cytochromeaa 3 are quinol oxidases. A fourth terminal oxidase, YthAB, is a putative quinol oxidase predicted from DNA sequence analysis. None of the terminal oxidases are, by themselves, essential for growth. However, one quinol oxidase (cytochromeaa 3 or cytochrome bd) is required for aerobic growth of B. subtilis strain 168. Data indicating that cytochrome aa 3 is the major oxidase used by exponentially growing cells in minimal and rich medium are presented. We show that one of the two heme-copper oxidases, cytochrome caa 3 or cytochromeaa 3, is required for efficient sporulation ofB. subtilis strain 168 and that deletion of YthAB in a strain lacking cytochrome aa 3 makes the strain sporulation deficient.

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