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 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.

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

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.

Biophysical Characterization of Mesophyll and Bundle Sheath Chloroplasts Isolated From the Leaves of Eleusine coracana, an Aspartate-Type C4 Plant. II. Photosynthetic Electron Transfer and Energy Conservation Reactions

1976 ◽  
Vol 3 (2) ◽  
pp. 185 ◽  
Author(s):  
CKM Rathnam ◽  
VSR Das
Keyword(s):  
Electron Transfer ◽  
Selective Inhibition ◽  
Bundle Sheath ◽  
C4 Plant ◽  
Biophysical Characterization ◽  
Ps Ii ◽  
Total Leaf ◽  
Photochemical Activities ◽  
Cyclic Photophosphorylation ◽  
Photosynthetic Electron Transfer

Mesophyll and bundle sheath chloroplasts isolated from the leaves of E. coracana, an aspartate-type C4 plant, have been utilized to study various photochemical activities in an effort to understand their high rates of photosysnthetic CO2 fixation. Bundle sheath chloroplasts were relatively more active in the overall process of photosynthetic electron transfer from water to NADP. Though photosystem II (PS II) and the associated non-cyclic photophosphorylation activities were of the same magnitude in both types of chloroplast, PS I and the associated cyclic photophosphorylation activities were three to four times more active in bundle sheath chloroplasts than in mesophyll chloroplasts. The influence of different illuminance on the electron and energy transfer reactions has been studied. At all the light levels tested, cyclic photophosphorylation activity was higher than non-cyclic in bundle sheath chloroplasts, while sigmoid kinetics were observed with mesophyll chloroplasts. Acid-base phosphorylation activities of the two types of chloroplast were similar. Heat treatment of the chloroplasts resulted in a selective inhibition of PS II in both types. Total leaf chlorophyll was approximately equally destributed between mesophyll and bundle sheath chloroplasts, which were found to have chlorophyll a-chlorophyll b ratios of 4.50 and 3.50 respectively. A working hypothesis for the energy requirements in the mesophyll and bundle sheath cells for the maintenance of various biochemical processes is proposed. It is also concluded that a greater part of the total leaf photochemical potential is associated with bundle sheath chloroplasts of E. coracana.

Effect ofChlamydomonasplastid terminal oxidase 1 expressed in tobacco on photosynthetic electron transfer

2016 ◽  
Vol 85 (2) ◽  
pp. 219-228 ◽  
Author(s):  
Kathleen Feilke ◽  
Peter Streb ◽  
Gabriel Cornic ◽  
François Perreau ◽  
Jerzy Kruk ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Terminal Oxidase ◽  
Photosynthetic Electron Transfer

Respiratory Protection of Nitrogenase Activity in Azotobacter vinelandii—Roles of the Terminal Oxidases

1997 ◽  
Vol 17 (3) ◽  
pp. 303-317 ◽  
Author(s):  
Robert K. Poole ◽  
Susan Hill
Keyword(s):  
Gene Expression ◽  
Nitrogen Fixation ◽  
Oxygen Reduction ◽  
Crucial Role ◽  
Azotobacter Vinelandii ◽  
Nitrogenase Activity ◽  
Terminal Oxidase ◽  
Respiratory Protection ◽  
Terminal Oxidases ◽  
Cytochrome Bd

Nitrogen fixation by aerobic prokaryotes appears paradoxical: the nitrogen-fixing enzymes—nitrogenases—are notoriously oxygen-labile, yet many bacteria fix nitrogen aerobically. This review summarises the evidence that cytochrome bd, a terminal oxidase unrelated to the mitochondrial and many other bacterial oxidases, plays a crucial role in aerotolerant nitrogen fixation in Azotobacter vinelandii and other bacteria by rapidly consuming oxygen during uncoupled respiration. We review the pertinent properties of this oxidase, particularly its complement of redox centres, the catalytic cycle of oxygen reduction, the affinity of the oxidase for oxygen, and the regulation of cytochrome bd gene expression. The roles of other oxidases and other mechanisms for limiting damage to nitrogenase are assessed.

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.

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