scholarly journals In Organello and in Vivo Evidence of the Importance of the Regulatory Sulfhydryl/Disulfide System and Pyruvate for Alternative Oxidase Activity in Tobacco

1999 ◽  
Vol 121 (3) ◽  
pp. 793-803 ◽  
Author(s):  
Greg C. Vanlerberghe ◽  
Justine Y.H. Yip ◽  
Hannah L. Parsons
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase ◽  
In Organello

scholarly journals Regulation of Alternative Oxidase Activity in Six Wild Monocotyledonous Species. An in Vivo Study at the Whole Root Level

2001 ◽  
Vol 126 (1) ◽  
pp. 376-387 ◽  
Author(s):  
Frank F. Millenaar ◽  
Miquel A. Gonzàlez-Meler ◽  
Fabio Fiorani ◽  
Rob Welschen ◽  
Miquel Ribas-Carbo ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Alternative Oxidase ◽  
In Vivo Study

ИМПОРТ ДНК В МИТОХОНДРИИ РАСТЕНИЙ: КОМПЛЕКСНЫЙ ПОДХОД ДЛЯ ИЗУЧЕНИЯ in organello И in vivo

2019 ◽  
Vol 84 (7) ◽  
pp. 1036-1048
Author(s):  
Т.А. Тарасенко ◽  
В.И. Тарасенко ◽  
М.В. Кулинченко ◽  
Е.С. Клименко ◽  
Ю.М. Константинов
Keyword(s):  
In Organello

DNA Import into Plant Mitochondria: Complex Approach for in organello and in vivo Studies

2019 ◽  
Vol 84 (7) ◽  
pp. 817-828 ◽  
Author(s):  
T. A. Tarasenko ◽  
V. I. Tarasenko ◽  
M. V. Koulintchenko ◽  
E. S. Klimenko ◽  
Yu. M. Konstantinov
Keyword(s):  
Plant Mitochondria ◽  
In Vivo Studies ◽  
Complex Approach ◽  
In Organello

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 The Lack of Mitochondrial Thioredoxin TRXo1 Affects In Vivo Alternative Oxidase Activity and Carbon Metabolism under Different Light Conditions

2019 ◽  
Vol 60 (11) ◽  
pp. 2369-2381 ◽  
Author(s):  
Igor Florez-Sarasa ◽  
Toshihiro Obata ◽  
N�stor Fern�ndez Del-Saz ◽  
Jean-Philippe Reichheld ◽  
Etienne H Meyer ◽  
...  
Keyword(s):  
Carbon Metabolism ◽  
Redox State ◽  
Redox Regulation ◽  
Alternative Oxidase ◽  
Tricarboxylic Acid Cycle ◽  
Reduced Form ◽  
Photosynthetic Parameters ◽  
Primary Metabolism ◽  
Redox Systems

Abstract The alternative oxidase (AOX) constitutes a nonphosphorylating pathway of electron transport in the mitochondrial respiratory chain that provides flexibility to energy and carbon primary metabolism. Its activity is regulated in vitro by the mitochondrial thioredoxin (TRX) system which reduces conserved cysteines residues of AOX. However, in vivo evidence for redox regulation of the AOX activity is still scarce. In the present study, the redox state, protein levels and in vivo activity of the AOX in parallel to photosynthetic parameters were determined in Arabidopsis knockout mutants lacking mitochondrial trxo1 under moderate (ML) and high light (HL) conditions, known to induce in vivo AOX activity. In addition, 13C- and 14C-labeling experiments together with metabolite profiling were performed to better understand the metabolic coordination between energy and carbon metabolism in the trxo1 mutants. Our results show that the in vivo AOX activity is higher in the trxo1 mutants at ML while the AOX redox state is apparently unaltered. These results suggest that mitochondrial thiol redox systems are responsible for maintaining AOX in its reduced form rather than regulating its activity in vivo. Moreover, the negative regulation of the tricarboxylic acid cycle by the TRX system is coordinated with the increased input of electrons into the AOX pathway. Under HL conditions, while AOX and photosynthesis displayed similar patterns in the mutants, photorespiration is restricted at the level of glycine decarboxylation most likely as a consequence of redox imbalance.

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
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