Selective Oxidation of Nitric Oxide against Nitrite by Oxo-iron(IV) Porphyrin at an ITO Electrode

2003 ◽  
Vol 32 (7) ◽  
pp. 610-611 ◽  
Author(s):  
Jianping Lei ◽  
Natalia S. Trofimova ◽  
Osamu Ikeda
Keyword(s):  
Nitric Oxide ◽  
Selective Oxidation ◽  
Ito Electrode

Selective oxidation of methane in the presence of nitric oxide: comments on the reaction mechanism

1990 ◽  
Vol 6 (4) ◽  
pp. 399-407 ◽  
Author(s):  
Graham J. Hutchings ◽  
Michael S. Scurrell ◽  
Jeremy R. Woodhouse
Keyword(s):  
Nitric Oxide ◽  
Reaction Mechanism ◽  
Selective Oxidation ◽  
Oxidation Of Methane

Selective oxidation of nickel in copper-nickel alloys in nitric oxide

1975 ◽  
Vol 79 (14) ◽  
pp. 1480-1481 ◽  
Author(s):  
Yoshio Takasu ◽  
Yoshiharu Matsuda ◽  
Shunichi Maru ◽  
Nobutoshi Hayashi ◽  
Hiroshi Yoneyama ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Selective Oxidation ◽  
Nickel Alloys ◽  
Copper Nickel

Efficient Formation of Nitric Oxide from Selective Oxidation ofN-ArylN‘-Hydroxyguanidines by Inducible Nitric Oxide Synthase

Biochemistry ◽  
1999 ◽  
Vol 38 (15) ◽  
pp. 4663-4668 ◽  
Author(s):  
Axelle Renodon-Cornière ◽  
Jean-Luc Boucher ◽  
Sylvie Dijols ◽  
Dennis J. Stuehr ◽  
Daniel Mansuy
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Selective Oxidation ◽  
Inducible Nitric Oxide Synthase ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

N-ArylN‘-Hydroxyguanidines, A New Class of NO-Donors after Selective Oxidation by Nitric Oxide Synthases:  Structure−Activity Relationship

2002 ◽  
Vol 45 (4) ◽  
pp. 944-954 ◽  
Author(s):  
Axelle Renodon-Cornière ◽  
Sylvie Dijols ◽  
Céline Perollier ◽  
David Lefevre-Groboillot ◽  
Jean-Luc Boucher ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Selective Oxidation ◽  
Structure Activity Relationship ◽  
Nitric Oxide Synthases ◽  
Activity Relationship ◽  
No Donors ◽  
New Class ◽  
Structure Activity

Great adaptability of the heme-cysteinate monooxygenases family to very diverse substrates and sophisticated reactions

2007 ◽  
Vol 11 (04) ◽  
pp. 258-268
Author(s):  
Daniel Mansuy ◽  
Pierre Lafite
Keyword(s):  
Nitric Oxide ◽  
Selective Oxidation ◽  
Active Sites ◽  
Nitric Oxide Synthases ◽  
Dioxygen Activation ◽  
Chemical Environment ◽  
Huge Number ◽  
X Ray ◽  
Metabolism Of Xenobiotics ◽  
Cytochrome P 450

Heme-cysteinate proteins, such as cytochromes P 450( CYPs ) and nitric oxide synthases (NOSs), catalyze the monooxygenation of a huge number of substrates with very diverse structures. The ability of CYPs to oxidize a myriad of xenobiotics, in order to facilitate their elimination, plays a key role in the adaptation of aerobic organisms to their always changing chemical environment. Moreover, some members of the CYP superfamily and the NOSs are involved in the biosynthesis of key biological endogenous molecules, such as estrogens or NO, through the catalysis of highly sophisticated and regulated reactions. How can proteins using the same catalytic heme-cysteinate cofactor and mechanism of dioxygen activation oxidize such diverse and always changing substrates and catalyze different, sometimes very sophisticated reactions? Recent data on the first X-ray structures of mammalian cytochrome P 450-substrate complexes and on the mechanism of NO-synthases has permitted an understanding of this"double adaptation" of heme-cysteinate monooxygenases towards very diverse substrates and different reactions. These data show that cytochromes P 450 involved in the metabolism of xenobiotics are able to oxidize very different substrates by offering a great choice of very diverse and malleable active sites. They also show that heme-cysteinate monooxygenases are able to catalyze special, sophisticated reactions, such as the selective oxidation of L-arginine to NO, by using supplementary cofactors adapted for the required catalysis.

Localization of endothelial nitric oxide synthase in the normal and failing human atrial myocardium

1996 ◽  
Vol 54 ◽  
pp. 786-787
Author(s):  
Chi-Ming Wei ◽  
Margarita Bracamonte ◽  
Shi-Wen Jiang ◽  
Richard C. Daly ◽  
Christopher G.A. McGregor ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heart Failure ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Cardiac Tissues ◽  
Mammalian Tissues ◽  
End Stage Heart Failure ◽  
End Stage ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Nitric oxide (NO) is a potent endothelium-derived relaxing factor which also may modulate cardiomyocyte inotropism and growth via increasing cGMP. While endothelial nitric oxide synthase (eNOS) isoforms have been detected in non-human mammalian tissues, expression and localization of eNOS in the normal and failing human myocardium are poorly defined. Therefore, the present study was designed to investigate eNOS in human cardiac tissues in the presence and absence of congestive heart failure (CHF).Normal and failing atrial tissue were obtained from six cardiac donors and six end-stage heart failure patients undergoing primary cardiac transplantation. ENOS protein expression and localization was investigated utilizing Western blot analysis and immunohistochemical staining with the polyclonal rabbit antibody to eNOS (Transduction Laboratories, Lexington, Kentucky).

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