Comparative IR Study of Nitric Oxide Reactions with Sublimed Layers of Iron(II)− and Ruthenium(II)−meso-Tetraphenylporphyrinates

2002 ◽  
Vol 124 (34) ◽  
pp. 10124-10129 ◽  
Author(s):  
Tigran S. Kurtikyan ◽  
Garik G. Martirosyan ◽  
Ivan M. Lorkovic' ◽  
Peter C. Ford
1985 ◽  
Vol 89 (26) ◽  
pp. 5840-5845 ◽  
Author(s):  
Jim Liang ◽  
H. P. Wang ◽  
L. D. Spicer
Keyword(s):  
Ft Ir ◽  

2006 ◽  
Vol 10 (07) ◽  
pp. 971-977 ◽  
Author(s):  
Tigran S. Kurtikyan ◽  
Hayk A. Harutyunyan ◽  
Robert K. Ghazaryan ◽  
John A. Goodwin

The low-temperature interaction of NO(15NO ) with sublimed layers of meso-mono-4-pyridyl-tri-phenyl- and meso-mono-3-pyridyl-tri-phenyl-porphyrinatocobalt(II) ( CoM4PyTPP (I) and CoM3PyTPP (II), respectively) has been investigated by means of FTIR and UV-visible spectroscopy. In addition to the stable five-coordinate nitrosyl complexes that are similar to the closely-related meso-tetraphenylporphyrinatocobalt(II)-nitrosyl Co(TPP)(NO) complex, a new type of complex with coordinated NO (15 NO ) has been found for the layers that were maintained at room temperature overnight before addition of nitric oxide at low temperature. The ν{ NO (15 NO )} in this species are more than 20 cm−1 lower than in five-coordinate compounds. These adducts are assigned to six-coordinate nitrosyl complexes, in which the fifth coordination site is occupied by the pyridyl group of the adjacent I (II) molecules. Warming the layers containing six-coordinate nitrosyl complexes of I almost completely transforms them to stable five-coordinate nitrosyl species indicating oligomers' disruption rather than loss of nitric oxide. In the case of II, however, a noticeable fraction of the six-coordinate species is left upon warming. Introducing new portions of NO to these layers at low temperature leads to formation of additional quantities of the six-coordinate species. Hence, part of six-coordinate complexes in II decomposed upon warming by releasing NO instead of by breaking Co -pyridyl bonds, therefore leaving free the sixth coordination sites in these layers. This result suggests a good possibility for creating solid state NO storage devices in which nitrogen monoxide can be kept and easily released by warming of the system.


1986 ◽  
Vol 15 (12) ◽  
pp. 2003-2004 ◽  
Author(s):  
Toshiyuki Obara ◽  
Muneyoshi Yamada ◽  
Akira Amano
Keyword(s):  
Ft Ir ◽  

2010 ◽  
Vol 114 (40) ◽  
pp. 17092-17098 ◽  
Author(s):  
Jörg P. Thielemann ◽  
Jutta Kröhnert ◽  
Christian Hess

1988 ◽  
Vol 42 (4) ◽  
pp. 674-680 ◽  
Author(s):  
D. M. Smith ◽  
W. F. Welch ◽  
S. M. Graham ◽  
A. R. Chughtai ◽  
Brian G. Wicke ◽  
...  

Qualitative and quantitative studies of the reaction of black carbon with the oxides of nitrogen, including NO, NO2/N2O4, N2O, and N2O3, have been carried out with the use of Fourier transform infrared spectroscopy (FT-IR). The active reactant is shown to be NO2, whether it acts as a disproportionation product or as an impurity in the gas under study. FT-IR spectra of the surface species identify them as resulting from reaction of carbon with NO2. For paraffin candle soot which was exposed simultaneously to oxygen atoms, and nitric oxide at 298 K, the surface species also are due to NO2, formed by oxidative adsorption of NO on the soot surface.


Author(s):  
Chi-Ming Wei ◽  
Margarita Bracamonte ◽  
Shi-Wen Jiang ◽  
Richard C. Daly ◽  
Christopher G.A. McGregor ◽  
...  

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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