Nitric oxide and cellular respiration

Brunori, Maurizio; Giuffrè, Alessandro; Sarti, Paolo; Stubauer, Gottfried; Wilson, Michael T.

doi:10.1007/s000180050452

Cited by 80 publications

(49 citation statements)

References 53 publications

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“…Interaction of NO with cytochrome c oxidase (complex I) has dramatic biological consequences, such as the increase in the mitochondrial ROS level and the induction of apoptosis (Brunori et al, 1999). Therefore, the reason for NO toxicity is not a shutdown of respiration per se but an overreduction of the ubiquinone pool.…”

Section: Inhibition Of Gdc By Harpin and Nomentioning

confidence: 99%

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

et al. 2010

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Mitochondria play an essential role in nitric oxide (NO) signal transduction in plants. Using the biotin-switch method in conjunction with nano-liquid chromatography and mass spectrometry, we identified 11 candidate proteins that were S-nitrosylated and/or glutathionylated in mitochondria of Arabidopsis (Arabidopsis thaliana) leaves. These included glycine decarboxylase complex (GDC), a key enzyme of the photorespiratory C 2 cycle in C3 plants. GDC activity was inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues. Gas-exchange measurements demonstrated that the bacterial elicitor harpin, a strong inducer of reactive oxygen species and NO, inhibits GDC activity. Furthermore, an inhibitor of GDC, aminoacetonitrile, was able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells. These findings indicate that the mitochondrial photorespiratory system is involved in the regulation of NO signal transduction in Arabidopsis.

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Section: Inhibition Of Gdc By Harpin and Nomentioning

confidence: 99%

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

et al. 2010

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“…Mitochondrial respiration can be inhibited by both ONOO -and NO. With NO inhibition, an increase in ROS production by mitochondria has been observed (Brunori et al 1999). …”

Section: Mitochondrial Respirationmentioning

confidence: 99%

“…This is observed primarily in inflammation with activation of iNOS and increased iNOS NO production. iNOS is activated during inflammatory signaling and produces NO at high rates (Brunori et al 1999). This allows cells to be exposed to cytotoxic levels of NO.…”

Section: Nitric Oxidementioning

confidence: 99%

Mechanisms of H2O2-induced oxidative stress in endothelial cells

Coyle

Martínez

Coleman

et al. 2006

Free Radical Biology and Medicine

131

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“…The reactions of cytochrome c oxidase with nitric oxide (NO) have recently been the subject of renewed scrutiny (1-6) because of their emerging physiological significance (7)(8)(9)(10)(11)(12). Furthermore, the discovery and functional characterization of a mitochondrial NO synthase (9,13,14) raises a series of questions regarding the possible regulation of the electron transport chain by NO.…”

mentioning

confidence: 99%

Reversal of Cyanide Inhibition of Cytochrome c Oxidase by the Auxiliary Substrate Nitric Oxide

Pearce

Bominaar

Hill

et al. 2003

Journal of Biological Chemistry

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Nitric oxide (NO) is shown to overcome the cyanide inhibition of cytochrome c oxidase in the presence of excess ferrocytochrome c and oxygen. Addition of NO to the partially reduced cyanide-inhibited form of the bovine enzyme is shown by electron paramagnetic resonance spectroscopy to result in substitution of cyanide at ferriheme a 3 by NO with reduction of the heme. The resulting nitrosylferroheme a 3 is a 5-coordinate structure, the proximal bond to histidine having been broken. NO does not simply act as a reversibly bound competitive inhibitor but is an auxiliary substrate consumed in a catalytic cycle along with ferrocytochrome c and oxygen. The implications of this observation with regard to estimates of steady-state NO levels in vivo is discussed. Given the multiple sources of NO available to mitochondria, the present results appear to explain in part some of the curious biomedical observations reported by other laboratories; for example, the kidneys of cyanide poisoning victims surprisingly exhibit no significant irreversible damage, and lethal doses of potassium cyanide are able to inhibit cytochrome c oxidase activity by only ϳ50% in brain mitochondria.The reactions of cytochrome c oxidase with nitric oxide (NO) have recently been the subject of renewed scrutiny (1-6) because of their emerging physiological significance (7-12). Furthermore, the discovery and functional characterization of a mitochondrial NO synthase (9, 13, 14) raises a series of questions regarding the possible regulation of the electron transport chain by NO. Several catalytic cycles have been proposed (4,6,(15)(16)(17) to explain the consumption of NO by the oxidase while turning over in the presence of cytochrome c and oxygen. Some of these cycles implicitly treat the NO as an auxiliary substrate rather than simply a competitive inhibitor, to account for the observed production of nitrite in addition to the slowing of electron transfer rate. In some cases an oxyferryl intermediate of heme a 3 is proposed and interaction of incoming NO with Cu B assumed (15, 16), whereas other schemes invoke the formation of a nitrosylheme a 3 intermediate (4,6,17). Consequently, clarification of which (if either) of the two centers of the binuclear pair, heme a 3 or Cu B , preferentially reacts with NO to form detectable derivatives should be of some value in assessing the relative likelihood of one proposed scheme over another as conditions are varied.When metalloenzymes have multiple binding sites for small molecular substrates and inhibitors, especially within the same active site domain, studies with mixed-ligand adducts can often reveal useful details of the coordination chemistry. Here we report the results of an investigation into the preferred site of NO reaction with bovine heart cytochrome c oxidase in the presence of the potent competitive inhibitor, cyanide, both under conditions of turnover and where the enzyme has been allowed to equilibrate in the presence of NO, cyanide, and reducing equivalents. The findings we report appear to be ...

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Nitric oxide and cellular respiration

Cited by 80 publications

References 53 publications

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

Mechanisms of H2O2-induced oxidative stress in endothelial cells

Reversal of Cyanide Inhibition of Cytochrome c Oxidase by the Auxiliary Substrate Nitric Oxide

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