Nitric oxide ejects electrons from the binuclear centre of cytochrome <i>c</i> oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide?

Cooper, Chris E.; Torres, Jaume; Sharpe, Martyn A.; Wilson, Michael T.

doi:10.1016/s0014-5793(97)01009-0

Cited by 102 publications

(17 citation statements)

References 34 publications

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“…There is little argument that mitochondria contain bioactive NO— they do, as determined by the presence and formation of nitrosyl heme and copper [23], nitrated proteins [24], and S-nitrosothiols [25] as well as by SNO clearance or denitrosylating mechanisms [26]. …”

Section: Sources Of No In Mitochondriamentioning

confidence: 99%

Regulation of mitochondrial processes by protein S-nitrosylation

Piantadosi

2012

Biochimica et Biophysica Acta (BBA) - General Subjects

126

102

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Background Nitric oxide (NO) exerts powerful physiological effects through guanylate cyclase (GC), a non-mitochondrial enzyme, and through the generation of protein cysteinyl-NO (SNO) adducts— a post-translational modification relevant to mitochondrial biology. A small number of SNO proteins, generated by various mechanisms, are characteristically found in mammalian mitochondria and influence the regulation of oxidative phosphorylation and other aspects of mitochondrial function. Scope of Review The principles by which mitochondrial SNO proteins are formed and their actions, independently or collectively with NO binding to heme, iron-sulfur centers, or to glutathione (GSH) are reviewed on a molecular background of SNO-based signal transduction. Major Conclusions Mitochondrial SNO-proteins have been demonstrated to inhibit Complex I of the electron transport chain, to modulate mitochondrial reactive oxygen species (ROS) production, influence calcium-dependent opening of the mitochondrial permeability transition pore (MPTP), promote selective importation of mitochondrial protein, and stimulate mitochondrial fission. The ease of reversibility and the affirmation of regulated S-nitros(yl)ating and denitros(yl)ating enzymatic reactions supports hypotheses that SNO regulates the mitochondrion through redox mechanisms. SNO modification of mitochondrial proteins, whether homeostatic or adaptive (physiological), or pathogenic, is an area of active investigation. General Significance Mitochondrial SNO proteins are associated with mainly protective, bur soem pathological effects; the former mainly in inflammatory and ischemia/reperfusion syndromes and the latter in neurodegenerative diseases. Experimentally, mitochondrial SNO delivery is also emerging as a potential new area of therapeutics.

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Section: Sources Of No In Mitochondriamentioning

confidence: 99%

Regulation of mitochondrial processes by protein S-nitrosylation

Piantadosi

2012

Biochimica et Biophysica Acta (BBA) - General Subjects

126

102

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“…Later on this reaction was reinvestigated by Cooper et al [41] and Giuffrè et al [42], using a pulsed ( fast ) preparation of CcOX. The pulsing procedure that in vitro consists in preliminary reduction-reoxidation of CcOX [43], removes chloride from the oxidized active site of the enzyme thereby allowing fast reaction with NO [42]; indeed, CcOX is expectedly in the pulsed state in vivo where CcOX turnover takes place continuously.…”

Section: The Role Of Cub In the Reaction With Nomentioning

confidence: 99%

“…As a matter of fact, these standard culture conditions favor the overall accumulation of the CcOX intermediates P , F and O [29, 41, 42, 58]; these are the species responsible for the NO oxidation to nitrite. Consistently, upon rapid and efficient scavenging of bulk NO, respiration is promptly recovered.…”

Section: Cells Respiring In the Presence Of No And Using Endogenoumentioning

confidence: 99%

The Chemical Interplay between Nitric Oxide and Mitochondrial CytochromecOxidase: Reactions, Effectors and Pathophysiology

Sarti

Forte

Giuffrè

et al. 2012

International Journal of Cell Biology

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Nitric oxide (NO) reacts with Complex I and cytochrome c oxidase (CcOX, Complex IV), inducing detrimental or cytoprotective effects. Two alternative reaction pathways (PWs) have been described whereby NO reacts with CcOX, producing either a relatively labile nitrite-bound derivative (CcOX-NO2 −, PW1) or a more stable nitrosyl-derivative (CcOX-NO, PW2). The two derivatives are both inhibited, displaying different persistency and O2 competitiveness. In the mitochondrion, during turnover with O2, one pathway prevails over the other one depending on NO, cytochrome c 2+ and O2 concentration. High cytochrome c 2+, and low O2 proved to be crucial in favoring CcOX nitrosylation, whereas under-standard cell-culture conditions formation of the nitrite derivative prevails. All together, these findings suggest that NO can modulate physiologically the mitochondrial respiratory/OXPHOS efficiency, eventually being converted to nitrite by CcOX, without cell detrimental effects. It is worthy to point out that nitrite, far from being a simple oxidation byproduct, represents a source of NO particularly important in view of the NO cell homeostasis, the NO production depends on the NO synthases whose activity is controlled by different stimuli/effectors; relevant to its bioavailability, NO is also produced by recycling cell/body nitrite. Bioenergetic parameters, such as mitochondrial ΔΨ, lactate, and ATP production, have been assayed in several cell lines, in the presence of endogenous or exogenous NO and the evidence collected suggests a crucial interplay between CcOX and NO with important energetic implications.

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“…Contrary to the simple on/off mechanism observed in the competitive model, bound • NO reduces the enzyme and is itself oxidized to NO 2 − . Enzyme inhibition is reverted by dissociation of NO 2 − upon further reduction [88, 89]. This uncompetitive inhibition mechanism is favored by high [O 2 ] and low turnover and its main biological role seems to be to consume • NO, thus shaping • NO concentration dynamics in the tissue [90, 91].…”

Section: The Transient •No Change From the Background And The Mechmentioning

confidence: 99%

Nitric Oxide Inactivation Mechanisms in the Brain: Role in Bioenergetics and Neurodegeneration

Santos

Lourenço

Ledo

et al. 2012

International Journal of Cell Biology

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During the last decades nitric oxide (•NO) has emerged as a critical physiological signaling molecule in mammalian tissues, notably in the brain. •NO may modify the activity of regulatory proteins via direct reaction with the heme moiety, or indirectly, via S-nitrosylation of thiol groups or nitration of tyrosine residues. However, a conceptual understanding of how •NO bioactivity is carried out in biological systems is hampered by the lack of knowledge on its dynamics in vivo. Key questions still lacking concrete and definitive answers include those related with quantitative issues of its concentration dynamics and diffusion, summarized in the how much, how long, and how far trilogy. For instance, a major problem is the lack of knowledge of what constitutes a physiological •NO concentration and what constitutes a pathological one and how is •NO concentration regulated. The ambient •NO concentration reflects the balance between the rate of synthesis and the rate of breakdown. Much has been learnt about the mechanism of •NO synthesis, but the inactivation pathways of •NO has been almost completely ignored. We have recently addressed these issues in vivo on basis of microelectrode technology that allows a fine-tuned spatial and temporal measurement •NO concentration dynamics in the brain.

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Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide?

Cited by 102 publications

References 34 publications

Regulation of mitochondrial processes by protein S-nitrosylation

Regulation of mitochondrial processes by protein S-nitrosylation

The Chemical Interplay between Nitric Oxide and Mitochondrial CytochromecOxidase: Reactions, Effectors and Pathophysiology

Nitric Oxide Inactivation Mechanisms in the Brain: Role in Bioenergetics and Neurodegeneration

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