scholarly journals The opposite prognostic effect of NDUFS1 and NDUFS8 in lung cancer reflects the oncojanus role of mitochondrial complex I

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Chia-Yi Su ◽  
Yu-Chan Chang ◽  
Chih-Jen Yang ◽  
Ming-Shyan Huang ◽  
Michael Hsiao
Keyword(s):  
Lung Cancer ◽  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Prognostic Effect

Heterocyclic Analogues of Squamocin as Inhibitors of Mitochondrial Complex I. On the Role of the Terminal Lactone of Annonaceous Acetogenins

Biochemistry ◽  
2006 ◽  
Vol 45 (8) ◽  
pp. 2721-2728 ◽  
Author(s):  
Romain A. Duval ◽  
Guy Lewin ◽  
Eva Peris ◽  
Nadia Chahboune ◽  
Aurelio Garofano ◽  
...  
Keyword(s):  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Annonaceous Acetogenins

scholarly journals Molecular mechanism and physiological role of active–deactive transition of mitochondrial complex I

2013 ◽  
Vol 41 (5) ◽  
pp. 1325-1330 ◽  
Author(s):  
Marion Babot ◽  
Alexander Galkin
Keyword(s):  
Complex I ◽  
Physiological Role ◽  
Protective Mechanism ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
The Status ◽  
Nitric Oxide Metabolites

The unique feature of mitochondrial complex I is the so-called A/D transition (active–deactive transition). The A-form catalyses rapid oxidation of NADH by ubiquinone (k ~104 min−1) and spontaneously converts into the D-form if the enzyme is idle at physiological temperatures. Such deactivation occurs in vitro in the absence of substrates or in vivo during ischaemia, when the ubiquinone pool is reduced. The D-form can undergo reactivation given both NADH and ubiquinone availability during slow (k ~1–10 min−1) catalytic turnover(s). We examined known conformational differences between the two forms and suggested a mechanism exerting A/D transition of the enzyme. In addition, we discuss the physiological role of maintaining the enzyme in the D-form during the ischaemic period. Accumulation of the D-form of the enzyme would prevent reverse electron transfer from ubiquinol to FMN which could lead to superoxide anion generation. Deactivation would also decrease the initial burst of respiration after oxygen reintroduction. Therefore the A/D transition could be an intrinsic protective mechanism for lessening oxidative damage during the early phase of reoxygenation. Exposure of Cys39 of mitochondrially encoded subunit ND3 makes the D-form susceptible for modification by reactive oxygen species and nitric oxide metabolites which arrests the reactivation of the D-form and inhibits the enzyme. The nature of thiol modification defines deactivation reversibility, the reactivation timescale, the status of mitochondrial bioenergetics and therefore the degree of recovery of the ischaemic tissues after reoxygenation.

scholarly journals S100A4 alters metabolism and promotes invasion of lung cancer cells by up-regulating mitochondrial complex I protein NDUFS2

2019 ◽  
Vol 294 (18) ◽  
pp. 7516-7527 ◽  
Author(s):  
Lili Liu ◽  
Lei Qi ◽  
Teresa Knifley ◽  
Dava W. Piecoro ◽  
Piotr Rychahou ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cancer Cells ◽  
Complex I ◽  
Lung Cancer Cells ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex

scholarly journals Antioxidant effect of exercise: Exploring the role of the mitochondrial complex I superassembly

Redox Biology ◽  
2017 ◽  
Vol 13 ◽  
pp. 477-481 ◽  
Author(s):  
J.R. Huertas ◽  
S. Al Fazazi ◽  
A. Hidalgo-Gutierrez ◽  
L.C. López ◽  
R.A. Casuso
Keyword(s):  
Complex I ◽  
Antioxidant Effect ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex

Accessory subunits of mitochondrial complex I

2013 ◽  
Vol 41 (5) ◽  
pp. 1272-1279 ◽  
Author(s):  
Katarzyna Kmita ◽  
Volker Zickermann
Keyword(s):  
Molecular Mass ◽  
Complex I ◽  
Proton Translocation ◽  
Present Review ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Cellular Functions ◽  
Accessory Subunits

Mitochondrial complex I has a molecular mass of almost 1 MDa and comprises more than 40 polypeptides. Fourteen central subunits harbour the bioenergetic core functions. We are only beginning to understand the significance of the numerous accessory subunits. The present review addresses the role of accessory subunits for assembly, stability and regulation of complex I and for cellular functions not directly associated with redox-linked proton translocation.

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