scholarly journals Substrate kinetics of the alternative oxidase of Neurospora crassa

1980 ◽  
Vol 186 (3) ◽  
pp. 1009-1011 ◽  
Author(s):  
J Vanderleyden ◽  
C Peeters ◽  
H Verachtert ◽  
H Bertrand
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Submitochondrial Particles ◽  
Succinate Oxidation ◽  
Complex Ii ◽  
Ubiquinone Oxidoreductase ◽  
Kinetics Of ◽  
Substrate Kinetics

The kinetics of the succinate oxidation by cyanide-sensitive and cyanide-insensitive submitochondrial particles of Neurospora crassa cells suggest that both respiratory pathways use the same complex II. This is confirmed by comparing the kinetics of the reductase activities of the isolated succinate-ubiquinone oxidoreductase (complex II) of cyanide-sensitive and cyanide-insensitive cells respectively. No alternative-oxidase activity was found to be associated with the isolated complex II of cyanide-insensitive cells.

scholarly journals Stimulation of the alternative oxidase of Neurospora crassa by Nucleoside phosphates

1980 ◽  
Vol 188 (1) ◽  
pp. 141-144 ◽  
Author(s):  
J Vanderleyden ◽  
C Peeters ◽  
H Verachtert ◽  
H Bertrand
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Purine Nucleoside ◽  
Submitochondrial Particles ◽  
Fold Stimulation ◽  
Succinate Oxidase ◽  
Stimulation Of

The alternative-oxidase-mediated succinate oxidase activity of Neurospora crassa decreases drastically when mitochondria are fractionated into submitochondrial particles or treated with deoxycholate. The activity, however, can be completely restored in the presence of nucleoside 5′-monophosphates. The purine nucleoside 5′-monophosphates are more effective than the pyrimidine homologues. 5′-GMP gives a 10-fold stimulation of the alternative-oxidase-mediated succinate oxidase activity in submitochondrial particles. A comparison is made with the results obtained earlier with Moniliella tomentosa [Hanssens & Verachtert (1976) J. Bacteriol. 125, 825–835; Vanderleyden, Van Den Eynde & Verachtert (1980) Biochem. J. 186, 309–316].

scholarly journals Immunological identification of the alternative oxidase of Neurospora crassa mitochondria.

1989 ◽  
Vol 9 (3) ◽  
pp. 1362-1364 ◽  
Author(s):  
A M Lambowitz ◽  
J R Sabourin ◽  
H Bertrand ◽  
R Nickels ◽  
L McIntosh
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Hydroxamic Acid ◽  
Alternative Oxidase ◽  
Fungal Species ◽  
The Other ◽  
Wild Type ◽  
Higher Plant ◽  
Sauromatum Guttatum ◽  
Immunological Identification

Neurospora crassa mitochondria use a branched electron transport system in which one branch is a conventional cytochrome system and the other is an alternative cyanide-resistant, hydroxamic acid-sensitive oxidase that is induced when the cytochrome system is impaired. We used a monoclonal antibody to the alternative oxidase of the higher plant Sauromatum guttatum to identify a similar set of related polypeptides (Mr, 36,500 and 37,000) that was associated with the alternative oxidase activity of N. crassa mitochondria. These polypeptides were not present constitutively in the mitochondria of a wild-type N. crassa strain, but were produced in high amounts under conditions that induced alternative oxidase activity. Under the same conditions, mutants in the aod-1 gene, with one exception, produced apparently inactive alternative oxidase polypeptides, whereas mutants in the aod-2 gene failed to produce these polypeptides. The latter findings support the hypothesis that aod-1 is a structural gene for the alternative oxidase and that the aod-2 gene encodes a component that is required for induction of alternative oxidase activity. Finally, our results indicate that the alternative oxidase is highly conserved, even between plant and fungal species.

scholarly journals Substrate Kinetics of the Plant Mitochondrial Alternative Oxidase and the Effects of Pyruvate

1997 ◽  
Vol 115 (3) ◽  
pp. 1145-1153 ◽  
Author(s):  
MHN. Hoefnagel ◽  
P. R. Rich ◽  
Q. Zhang ◽  
J. T. Wiskich
Keyword(s):  
Alternative Oxidase ◽  
Kinetics Of ◽  
Substrate Kinetics

Immunological identification of the alternative oxidase of Neurospora crassa mitochondria

1989 ◽  
Vol 9 (3) ◽  
pp. 1362-1364
Author(s):  
A M Lambowitz ◽  
J R Sabourin ◽  
H Bertrand ◽  
R Nickels ◽  
L McIntosh
Keyword(s):  
Neurospora Crassa ◽  
Oxidase Activity ◽  
Hydroxamic Acid ◽  
Alternative Oxidase ◽  
Fungal Species ◽  
The Other ◽  
Wild Type ◽  
Higher Plant ◽  
Sauromatum Guttatum ◽  
Immunological Identification

Neurospora crassa mitochondria use a branched electron transport system in which one branch is a conventional cytochrome system and the other is an alternative cyanide-resistant, hydroxamic acid-sensitive oxidase that is induced when the cytochrome system is impaired. We used a monoclonal antibody to the alternative oxidase of the higher plant Sauromatum guttatum to identify a similar set of related polypeptides (Mr, 36,500 and 37,000) that was associated with the alternative oxidase activity of N. crassa mitochondria. These polypeptides were not present constitutively in the mitochondria of a wild-type N. crassa strain, but were produced in high amounts under conditions that induced alternative oxidase activity. Under the same conditions, mutants in the aod-1 gene, with one exception, produced apparently inactive alternative oxidase polypeptides, whereas mutants in the aod-2 gene failed to produce these polypeptides. The latter findings support the hypothesis that aod-1 is a structural gene for the alternative oxidase and that the aod-2 gene encodes a component that is required for induction of alternative oxidase activity. Finally, our results indicate that the alternative oxidase is highly conserved, even between plant and fungal species.

scholarly journals Respiratory complex II: ROS production and the kinetics of ubiquinone reduction

2017 ◽  
Vol 1858 (2) ◽  
pp. 109-117 ◽  
Author(s):  
Vera G. Grivennikova ◽  
Vladimir S. Kozlovsky ◽  
Andrei D. Vinogradov
Keyword(s):  
Ros Production ◽  
Complex Ii ◽  
Respiratory Complex ◽  
Kinetics Of

scholarly journals Deficient cyclic adenosine 3',5'-monophosphate control in mutants of two genes of Neurospora crassa.

1981 ◽  
Vol 1 (1) ◽  
pp. 1-8 ◽  
Author(s):  
M L Pall ◽  
J M Trevillyan ◽  
N Hinman
Keyword(s):  
Plasma Membrane ◽  
Membrane Potential ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Neurospora Crassa ◽  
Alternative Oxidase ◽  
Oscillatory Behavior ◽  
Wild Type ◽  
Glucose Transport System ◽  
Regulated Functions

Strains of Neurospora crassa mutant in either of two genes, Crisp-1 (cr1) and Frost (fr), showed no increase of cyclic adenosine 3',5'-monophosphate (cyclic AMP) levels when subjected to several treatments which produce large increases of cyclic AMP in wild-type Neurospora. Evidently, the previously reported deficiencies of adenylate cyclase in these mutants were sufficient to block the normal increases. This fact suggests that both mutants could be used to help determine which control phenomena involve cyclic AMP and to interrupt the control of established cyclic AMP-regulated functions. Earlier studies had suggested an interdependence of the cyclic AMP level and the electric potential difference across the plasma membrane of Neurospora. Present experiments, therefore, employed several strains with the cr1 mutation to test for possible roles of cyclic AMP in recovery and oscillatory behavior of the Neurospora membrane potential. The results showed all such phenomena to be normal in the adenylate cyclase-defective strains, which demonstrates that variations of cyclic AMP are not obligatorily involved in the apparent control processes. Evidence is also presented that the induction of both glucose transport system II and the alternative oxidase do not require elevated cyclic AMP levels.

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