A Plethora of Terminal Oxidases and Their Biogenesis Factors inBradyrhizobium japonicum

2015 ◽  
pp. 293-306 ◽  
Author(s):  
Zeb A. Youard ◽  
Helge K. Abicht ◽  
Elisabeth Mohorko ◽  
Fabio Serventi ◽  
Eugenia Rigozzi ◽  
...  
Keyword(s):  
Terminal Oxidases

Ferrous iron oxidation in moderately thermophilic acidophile Sulfobacillus sibiricus N1T

2010 ◽  
Vol 56 (10) ◽  
pp. 803-808 ◽  
Author(s):  
Tatiana Y. Dinarieva ◽  
Anna E. Zhuravleva ◽  
Oksana A. Pavlenko ◽  
Iraida A. Tsaplina ◽  
Alexander I. Netrusov
Keyword(s):  
Ferrous Iron ◽  
High Performance ◽  
Iron Oxidation ◽  
Early Exponential Phase ◽  
Moderately Thermophilic ◽  
Terminal Oxidases ◽  
Cytochrome Bo ◽  
Ferrous Iron Oxidation ◽  
Transport Chain ◽  
Membrane Bound

The iron-oxidizing system of a moderately thermophilic, extremely acidophilic, gram-positive mixotroph, Sulfobacillus sibiricus N1T, was studied by spectroscopic, high-performance liquid chromatography and inhibitory analyses. Hemes B, A, and O were detected in membranes of S. sibiricus N1T. It is proposed that the electron transport chain from Fe2+ to O2 is terminated by 2 physiological oxidases: aa3-type cytochrome, which dominates in the early-exponential phase of growth, and bo3-type cytochrome, whose role in iron oxidation becomes more prominent upon growth of the culture. Both oxidases were sensitive to cyanide and azide. Cytochrome aa3 was more sensitive to cyanide and azide, with Ki values of 4.1 and 2.5 µmol·L–1, respectively, compared with Ki values for cytochrome bo3, which were 9.5 µmol·L–1 for cyanide and 7.0 µmol·L–1 for azide. This is the first evidence for the participation of a bo3-type oxidase in ferrous iron oxidation. The respiratory chain of the mixotroph contains, in addition to the 2 terminal oxidases, a membrane-bound cytochrome b573.

scholarly journals ROS Defense Systems and Terminal Oxidases in Bacteria

Antioxidants ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 839
Author(s):  
Vitaliy B. Borisov ◽  
Sergey A. Siletsky ◽  
Martina R. Nastasi ◽  
Elena Forte
Keyword(s):  
Defense Mechanisms ◽  
Protective Role ◽  
Superoxide Dismutases ◽  
Oxygen Species ◽  
Ros Scavenging ◽  
Terminal Oxidases ◽  
Defense Systems ◽  
Respiratory Chains ◽  
Scavenging Enzymes

Reactive oxygen species (ROS) comprise the superoxide anion (O2·−), hydrogen peroxide (H2O2), hydroxyl radical (·OH), and singlet oxygen (1O2). ROS can damage a variety of macromolecules, including DNA, RNA, proteins, and lipids, and compromise cell viability. To prevent or reduce ROS-induced oxidative stress, bacteria utilize different ROS defense mechanisms, of which ROS scavenging enzymes, such as superoxide dismutases, catalases, and peroxidases, are the best characterized. Recently, evidence has been accumulating that some of the terminal oxidases in bacterial respiratory chains may also play a protective role against ROS. The present review covers this role of terminal oxidases in light of recent findings.

scholarly journals Expression of terminal oxidases under nutrient-limited conditions in Shewanella oneidensis MR-1

2014 ◽  
Vol 1837 ◽  
pp. e99-e100
Author(s):  
Sébastien Le Laz ◽  
Arlette Kpebe ◽  
Marielle Bauzan ◽  
Sabrina Lignon ◽  
Marc Rousset ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Terminal Oxidases

scholarly journals Thylakoid Terminal Oxidases Are Essential for the Cyanobacterium Synechocystis sp. PCC 6803 to Survive Rapidly Changing Light Intensities

2013 ◽  
Vol 162 (1) ◽  
pp. 484-495 ◽  
Author(s):  
David J. Lea-Smith ◽  
Nic Ross ◽  
Maria Zori ◽  
Derek S. Bendall ◽  
John S. Dennis ◽  
...  
Keyword(s):  
Terminal Oxidases ◽  
Light Intensities ◽  
Changing Light ◽  
Synechocystis Sp ◽  
Pcc 6803

Effect of Growth Conditions on the Synthesis of Terminal Oxidases in Methylobacillus flagellatus KT

2002 ◽  
Vol 398 (1) ◽  
pp. 118-124 ◽  
Author(s):  
Maria S Muntyan ◽  
Tatiana Yu. Dinarieva ◽  
Mark V Baev ◽  
Alexander I Netrusov
Keyword(s):  
Growth Conditions ◽  
Terminal Oxidases

scholarly journals The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase

1972 ◽  
Vol 129 (3) ◽  
pp. 755-761 ◽  
Author(s):  
M. V. Jones ◽  
D. E. Hughes
Keyword(s):  
Electron Transport ◽  
Nicotinic Acid ◽  
Electron Transport Chain ◽  
Acid Oxidase ◽  
Terminal Oxidase ◽  
Difference Spectra ◽  
Terminal Oxidases ◽  
Cytochrome O ◽  
Transport Chain ◽  
Terminal Oxidation

In cell-free extracts of Pseudomonas ovalis nicotinic acid oxidase is confined to the wallmembrane fraction. It is associated with an electron-transport chain comprising b- and c-type cytochromes only, differing proportions of which are reduced by nicotinate and NADH. CO difference-spectra show two CO-binding pigments, cytochrome o (absorption maximum at 417nm) and another component absorbing maximally at 425nm. Cytochrome o is not reduced by NADH or by succinate but is by nicotinate, which can also reduce the ‘425’ CO-binding pigment. The effects of inhibitors of terminal oxidation support the idea of two terminal oxidases and a scheme involving the ‘425’ CO-binding pigment and the other components of the electron-transport chain is proposed.

scholarly journals Terminal oxidases ofCrithidia oncopelti

1984 ◽  
Vol 21 (3) ◽  
pp. 319-322 ◽  
Author(s):  
C. Edwards
Keyword(s):  
Terminal Oxidases
Sign in / Sign up

Export Citation Format

Share Document