Defining the Structural Domain of Subunit II of the Heme-Copper Terminal Oxidase Using Chimeric Enzymes Constructed from the Escherichia coli bo-Type Ubiquinol Oxidase and the Thermophilic Bacillus caa3-Type Cytochrome c Oxidase

1999 ◽  
Vol 126 (5) ◽  
pp. 934-939 ◽  
Author(s):  
K. Sakamoto ◽  
T. Mogi ◽  
S. Noguchi ◽  
N. Sone
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Structural Domain ◽  
Terminal Oxidase ◽  
Thermophilic Bacillus ◽  
Chimeric Enzymes ◽  
Ubiquinol Oxidase

A novel a-type terminal oxidase from Sulfolobusacidocaldarius with cytochrome c oxidase activity

1989 ◽  
Vol 165 (3) ◽  
pp. 1110-1114 ◽  
Author(s):  
Takayoshi Wakagi ◽  
Tatsuo Yamauchi ◽  
Tairo Oshima ◽  
Michele Müller ◽  
Angello Azzi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Terminal Oxidase

Cytochrome aa3 in facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense

2005 ◽  
Vol 51 (8) ◽  
pp. 621-627 ◽  
Author(s):  
Takuro Nunoura ◽  
Yoshihiko Sako ◽  
Takayoshi Wakagi ◽  
Aritsune Uchida
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Gene Product ◽  
Respiratory Chain ◽  
Oxidase Activity ◽  
Terminal Oxidase ◽  
Hyperthermophilic Archaeon ◽  
Consumption Activity ◽  
Copper Oxidase

We partially purified and characterized the cytochrome aa3 from the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense. This cytochrome aa3 showed oxygen consumption activity with N, N, N′, N′-tetramethyl-1,4-phenylenediamine and ascorbate as substrates, and also displayed bovine cytochrome c oxidase activity. These enzymatic activities of cytochrome aa3 were inhibited by cyanide and azide. This cytochrome contained heme As, but not typical heme A. An analysis of trypsin-digested fragments indicated that 1 subunit of this cytochrome was identical to the gene product of subunit I of the SoxM-type heme – copper oxidase (poxC). This is the first report of a terminal oxidase in hyperthermophilic crenarchaeon belonging to the order Thermoproteales.Key words: aerobic respiratory chain, terminal oxidase, Archaea, hyperthermophile, Pyrobaculum.

scholarly journals Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool

1984 ◽  
Vol 217 (2) ◽  
pp. 551-560 ◽  
Author(s):  
R J Froud ◽  
C I Ragan
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
State Level ◽  
Complex Iii ◽  
Molar Ratio ◽  
Cytochrome C Reductase ◽  
Molar Ratios ◽  
Ubiquinol Oxidase ◽  
Mediated Electron Transfer ◽  
Pool Model

Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely diffusible pool on the membrane. This model was based on that of Kröger & Klingenberg [(1973) Eur. J. Biochem. 34, 358-368] for ubiquinone-pool behaviour. Further confirmation of the pool model was provided by analysis of ubiquinol oxidase activity as a function of the molar ratio of the complexes and prediction of the degree of inhibition by antimycin.

scholarly journals Replacement of a terminal cytochrome c oxidase by ubiquinol oxidase during the evolution of acetic acid bacteria

2014 ◽  
Vol 1837 (10) ◽  
pp. 1810-1820 ◽  
Author(s):  
Minenosuke Matsutani ◽  
Kota Fukushima ◽  
Chiho Kayama ◽  
Misato Arimitsu ◽  
Hideki Hirakawa ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Acetic Acid Bacteria ◽  
Ubiquinol Oxidase

scholarly journals Properties of ubiquinol oxidase reconstituted from ubiquinol-cytochrome c reductase, cytochrome c and cytochrome c oxidase

1982 ◽  
Vol 202 (2) ◽  
pp. 527-534 ◽  
Author(s):  
R J Diggens ◽  
C I Ragan
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Maximal Activity ◽  
Complex Iii ◽  
Protein Ratio ◽  
Quinol Oxidase ◽  
Cytochrome C Reductase ◽  
Ubiquinol Oxidase ◽  
High Affinity

Ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase can be combined to reconstitute antimycin-sensitive ubiquinol oxidase activity. In 25 mM-acetate/Tris, pH 7.8, cytochrome c binds at high-affinity sites (KD = 0.1 microM) and low-affinity sites (KD approx. 10 microM). Quinol oxidase activity is 50% of maximal activity when cytochrome c is bound to only 25% of the high affinity sites. The other 50% of activity seems to be due to cytochrome c bound at low-affinity sites. Reconstitution in the presence of soya-bean phospholipids prevents aggregation of cytochrome c oxidase and gives rise to much higher rates of quinol oxidase. The cytochrome c dependence was unaltered. Antimycin curves have the same shape regardless of lipid/protein ratio, Complex III/cytochrome c oxidase ratio or cytochrome c concentration. Proposals on the nature of the interaction between Complex III, cytochrome c and cytochrome c oxidase are considered in the light of these results.

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