scholarly journals Alternative Oxidase Activity and the Ubiquinone Redox Level in Soybean Cotyledon and Arum Spadix Mitochondria during NADH and Succinate Oxidation

1996 ◽  
Vol 110 (4) ◽  
pp. 1329-1335 ◽  
Author(s):  
MHN. Hoefnagel ◽  
J. T. Wiskich
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Succinate Oxidation ◽  
Soybean Cotyledon ◽  
Redox Level

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].

Characterization of an alternative oxidase activity ofHistoplasma capsulatum

Yeast ◽  
2003 ◽  
Vol 20 (5) ◽  
pp. 381-388 ◽  
Author(s):  
Clayton H. Johnson ◽  
Jonathan T. Prigge ◽  
Aaron D. Warren ◽  
Joan E. McEwen
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase

scholarly journals Regulation of Alternative Oxidase Activity by Pyruvate in Soybean Mitochondria

1994 ◽  
Vol 106 (4) ◽  
pp. 1421-1427 ◽  
Author(s):  
D. A. Day ◽  
A. H. Millar ◽  
J. T. Wiskich ◽  
J. Whelan
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase

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 Identification of the quinone species in cyanide-sensitive and cyanide-insensitive mitochondria of Moniliella tomentosa

1980 ◽  
Vol 192 (3) ◽  
pp. 881-885 ◽  
Author(s):  
J Vanderleyden ◽  
M Meyers ◽  
H Verachtert
Keyword(s):  
Electron Transport ◽  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Transport Pathways ◽  
Naturally Occurring

Moniliella tomentosa was investigated for the presence of different quinones that might be involved in the cyanide-sensitive and/or cyanide-insensitive electron-transport pathways. The naturally occurring quinone in Moniliella tomentosa was found to be ubiquinone-45. Other quinone species could not be detected. The concentration of ubiquinone-45 in mitochondria is not related to the presence or absence of the alternative oxidase activity.

scholarly journals Kinetic analysis of the mitochondrial quinol-oxidizing enzymes during development of thermogenesis in Arum maculatum L

1996 ◽  
Vol 317 (1) ◽  
pp. 313-319 ◽  
Author(s):  
Graeme R. LEACH ◽  
Klaas KRAB ◽  
David G. WHITEHOUSE ◽  
Anthony L. MOORE
Keyword(s):  
Respiratory Rate ◽  
Succinate Dehydrogenase ◽  
Oxidase Activity ◽  
Alternative Oxidase ◽  
Alternative Pathway ◽  
Respiratory Control ◽  
Stage Of Development ◽  
Activation Level ◽  
Cytochrome Pathway ◽  
Arum Maculatum

The dependence of the rate of oxygen uptake upon the ubiquinone (Q)-pool reduction level in mitochondria isolated during the development of thermogenesis of Arum maculatum spadices has been investigated. At the α-stage of development, the respiratory rate was linearly dependent upon the reduction level of the Q-pool (Qr) both under state-3 and -4 conditions. Progression through the β/γ to the Δ-stage resulted in a non-linear dependence of the state-4 rate on Qr. In the Δ-stage of development, both state-3 and -4 respiratory rates were linearly dependent upon Qr due to a shift in the engagement of the alternative oxidase to lower levels of Qr. Western blot analysis revealed that increased alternative oxidase activity could be correlated with expression of a 35 kDa protein. Respiratory control was only observed with mitochondria in the α-stage of development. At the β/γ-stage of development, the addition of ADP resulted in a significant oxidation of the Q-pool which was accompanied by a decrease in the respiratory rate. This was due either to decreased contribution of the alternative pathway to the overall respiratory rate under state 3 or by deactivation of succinate dehydrogenase activity by ADP. Cold-storage of the spadices at the β-stage of development led to increased activity of both the cytochrome pathway and succinate dehydrogenase, without any change in alternative oxidase activity. Results are discussed in terms of how changes in the activation level of the alternative oxidase and succinate dehydrogenase influence the activity and engagement of the quinol-oxidizing pathways during the development of thermogenesis in A. maculatum.

scholarly journals Regulation of plant alternative oxidase activity: A tale of two cysteines

2006 ◽  
Vol 1757 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Ann L. Umbach ◽  
Vicki S. Ng ◽  
James N. Siedow
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase
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