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 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.

Terminal oxidases of cyanobacteria

2005 ◽  
Vol 33 (4) ◽  
pp. 832-835 ◽  
Author(s):  
S.E. Hart ◽  
B.G. Schlarb-Ridley ◽  
D.S. Bendall ◽  
C.J. Howe
Keyword(s):  
Electron Transfer ◽  
Electron Donors ◽  
Terminal Oxidase ◽  
Biophysical Characterization ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Cytochrome Bd ◽  
Genetic Level ◽  
Respiratory Oxidases ◽  
Photosynthetic Electron Transfer

The respiratory chain of cyanobacteria appears to be branched rather than linear; furthermore, respiratory and photosynthetic electron-transfer chains co-exist in the thylakoid membrane and even share components. This review will focus on the three types of terminal respiratory oxidases identified so far on a genetic level in cyanobacteria: aa3-type cytochrome c oxidase, cytochrome bd-quinol oxidase and the alternative respiratory terminal oxidase. We summarize here their genetic, biochemical and biophysical characterization to date and discuss their interactions with electron donors as well as their physiological roles.

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 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

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 Alternative oxidase: an inter-kingdom perspective on the function and regulation of this broadly distributed 'cyanide-resistant' terminal oxidase

2008 ◽  
Vol 35 (7) ◽  
pp. 535 ◽  
Author(s):  
Allison E. McDonald
Keyword(s):  
Translational Regulation ◽  
Alternative Oxidase ◽  
Physiological Function ◽  
Comparative Approach ◽  
Terminal Oxidase ◽  
Transcriptional Expression ◽  
Inner Mitochondrial Membrane ◽  
Respiratory Pathway ◽  
Quinol Oxidase ◽  
Transport Chain

Alternative oxidase (AOX) is a terminal quinol oxidase located in the respiratory electron transport chain that catalyses the oxidation of quinol and the reduction of oxygen to water. However, unlike the cytochrome c oxidase respiratory pathway, the AOX pathway moves fewer protons across the inner mitochondrial membrane to generate a proton motive force that can be used to synthesise ATP. The energy passed to AOX is dissipated as heat. This appears to be very wasteful from an energetic perspective and it is likely that AOX fulfils some physiological function(s) that makes up for its apparent energetic shortcomings. An examination of the known taxonomic distribution of AOX and the specific organisms in which AOX has been studied has been used to explore themes pertaining to AOX function and regulation. A comparative approach was used to examine AOX function as it relates to the biochemical function of the enzyme as a quinol oxidase and associated topics, such as enzyme structure, catalysis and transcriptional expression and post-translational regulation. Hypotheses that have been put forward about the physiological function(s) of AOX were explored in light of some recent discoveries made with regard to species that contain AOX. Fruitful areas of research for the AOX community in the future have been highlighted.

The Terminal Oxidase in the Marine Bacterium Pseudomonas nautica 617

1997 ◽  
Vol 17 (3) ◽  
pp. 343-346 ◽  
Author(s):  
Helen Simpson ◽  
Michel Denis ◽  
Francesco Malatesta
Keyword(s):  
Hydrogen Peroxide ◽  
Carbon Monoxide ◽  
Oxygen Reduction ◽  
Epr Spectroscopy ◽  
Marine Bacterium ◽  
Large Family ◽  
Terminal Oxidase ◽  
Quinol Oxidase ◽  
Terminal Oxidases ◽  
Production Of Hydrogen

The molecular properties of a novel membrane quinol oxidase from the marine bacterium Pseudomonas nautica 617 are presented. The protein contains 2b hemes/mole which may be distinguished by EPR spectroscopy but not by optical spectroscopy and electrochemistry. Respiration, though being cyanide insensitive, is not inhibited by carbon monoxide and oxygen reduction is carried out only half-way with production of hydrogen peroxide. The terminal oxidase represents, therefore, a unique example in the large family of terminal oxidases known up to date.

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