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Difference between revisions of "Sarti 2011 Biochim Biophys Acta"

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{{Publication
{{Publication
|title=Sarti P, Forte E, Mastronicola D, Giuffrè A, Arese M (2011) Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications. Biochim Biophys Acta [Epub ahead of print].
|title=Sarti P, Forte E, Mastronicola D, Giuffrè A, Arese M (2011) Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications. Biochim Biophys Acta 1817: 610-619
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21939634 PMID: 21939634]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21939634 PMID: 21939634]
|authors=Sarti P, Forte E, Mastronicola D, Giuffre A, Arese M
|authors=Sarti P, Forte E, Mastronicola D, Giuffre A, Arese M

Revision as of 15:34, 8 March 2013

Publications in the MiPMap
Sarti P, Forte E, Mastronicola D, Giuffrè A, Arese M (2011) Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications. Biochim Biophys Acta 1817: 610-619

» PMID: 21939634

Sarti P, Forte E, Mastronicola D, Giuffre A, Arese M (2011) Biochim Biophys Acta

Abstract: BACKGROUND: The reactions between Complex IV (cytochrome c oxidase, CcOX) and nitric oxide (NO) were described in the early 60's. The perception, however, that NO could be responsible for physiological or pathological effects, including those on mitochondria, lags behind the 80's, when the identity of the endothelial derived relaxing factor (EDRF) and NO synthesis by the NO synthases were discovered. NO controls mitochondrial respiration, and cytotoxic as well as cytoprotective effects have been described. The depression of OXPHOS ATP synthesis has been observed, attributed to the inhibition of mitochondrial Complex I and IV particularly, found responsible of major effects.

SCOPE OF REVIEW: The review is focused on CcOX and NO with some hints about pathophysiological implications. The reactions of interest are reviewed, with special attention to the molecular mechanisms underlying the effects of NO observed on cytochrome c oxidase, particularly during turnover with oxygen and reductants. MAJOR CONCLUSIONS AND

GENERAL SIGNIFICANCE: The NO inhibition of CcOX is rapid and reversible and may occur in competition with oxygen. Inhibition takes place following two pathways leading to formation of either a relatively stable nitrosyl-derivative (CcOX-NO) of the enzyme reduced, or a more labile nitrite-derivative (CcOX-NO(2)(-)) of the enzyme oxidized, and during turnover. The pathway that prevails depends on the turnover conditions and concentration of NO and physiological substrates, cytochrome c and O(2). All evidence suggests that these parameters are crucial in determining the CcOX vs NO reaction pathway prevailing in vivo, with interesting physiological and pathological consequences for cells. This article is part of a Special Issue entitled: Respiratory Oxidases. Keywords: endothelial derived relaxing factor (EDRF)

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Enzyme: Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property. 


HRR: Oxygraph-2k