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Difference between revisions of "Rodriguez-Juarez 2007 Biochem J"

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{{Publication
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|title=Rodriguez-Juarez F, Aguirre E, Cadenas S (2007) Relative sensitivity of soluble guanylate cyclase and mitochondrial respiration to endogenous nitric oxide at physiological oxygen concentration. Biochem. J. 405: 223-231.
|authors=Rodriguez-Juarez F, Aguirre E, Cadenas S
|year=2007
|journal=Biochem. J.
|abstract=Nitric oxide (NO) is a widespread biological messenger that has many physiological and pathophysiological roles. Most of the physiological actions of NO are mediated through the activation of sGC (soluble guanylate cyclase) and the subsequent production of cGMP. NO also binds to the binuclear centre of COX (cytochrome ''c'' oxidase) and inhibits mitochondrial respiration in competition with oxygen and in a reversible manner. Although sGC is more sensitive to endogenous NO than COX at atmospheric oxygen tension, the more relevant question is which enzyme is more sensitive at physiological oxygen concentration. Using a system in which NO is generated inside the cells in a finely controlled manner, we determined cGMP accumulation by immunoassay and mitochondrial oxygen consumption by high-resolution respirometry at 30 Β΅M oxygen. In the present paper, we report that the NO EC<sub>50</sub> of sGC was approx. 2.9 nM, whereas that required to achieve IC<sub>50</sub> of respiration was 141 nM (the basal oxygen consumption in the absence of NO was 14Β±0.8 pmol of O2/s per 106Β  cells). In accordance with this, the NO–cGMP signalling transduction pathway was activated at lower NO concentrations than the AMPKs (AMP-activated protein kinase) pathway. We conclude that sGC is approx. 50-fold more sensitive than cellular respiration to endogenous NO under our experimental conditions. The implications of these results for cell physiology are discussed.
|keywords=Cytochrome ''c'' oxidase, High-resolution respirometry, Mitochondrial respiration, Nitric oxide (NO), Oxygen consumption, Soluble guanylate cyclase.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17441787 PMID: 17441787]
}}
{{Labeling
|discipline=Mitochondrial Physiology, Biomedicine
|injuries=RONS; Oxidative Stress
|enzymes=Complex IV; Cytochrome c Oxidase
|kinetics=ADP; Pi, Oxygen, Reduced Substrate; Cytochrome c, Inhibitor; Uncoupler
|topics=Respiration; OXPHOS; ETS Capacity
|instruments=Oxygraph-2k
|articletype=Protocol; Manual
}}

Revision as of 18:50, 29 September 2010