A nitric oxide releaser based on the μ-oxo-hexaacetate-bis(4-methylpyridine)triruthenium nitrosyl complex

2005 ◽  
Vol 358 (10) ◽  
pp. 2891-2899 ◽  
Author(s):  
Henrique E. Toma ◽  
Anamaria D.P. Alexiou ◽  
André Luiz B. Formiga ◽  
Marcelo Nakamura ◽  
Sergio Dovidauskas ◽  
...  
Author(s):  
Niklas Gessner ◽  
Anna Karina Bäck ◽  
Johannes Knorr ◽  
Christoph Nagel ◽  
Philipp Marquetand ◽  
...  

Transition metal complexes capable of releasing small molecules such as carbon monoxide and nitric oxide upon photoactivation are versatile tools in various fields of chemistry and biology. In this work,...


1995 ◽  
Vol 270 (39) ◽  
pp. 22997-23006 ◽  
Author(s):  
Husam M. Abu-Soud ◽  
Jianling Wang ◽  
Denis L. Rousseau ◽  
Jon M. Fukuto ◽  
Louis J. Ignarro ◽  
...  

2005 ◽  
Vol 127 (40) ◽  
pp. 13758-13759 ◽  
Author(s):  
Raju Prakash ◽  
Alexander U. Czaja ◽  
Frank W. Heinemann ◽  
Dieter Sellmann

2008 ◽  
Vol 5 (3) ◽  
pp. 389-398 ◽  
Author(s):  
Qingdong Zheng ◽  
Adela Bonoiu ◽  
Tymish Y. Ohulchanskyy ◽  
Guang S. He ◽  
Paras N. Prasad

2008 ◽  
Vol 457 (2) ◽  
pp. 271-279 ◽  
Author(s):  
Karol Ondrias ◽  
Andrej Stasko ◽  
Sona Cacanyiova ◽  
Zdena Sulova ◽  
Olga Krizanova ◽  
...  

2006 ◽  
Vol 128 (11) ◽  
pp. 3831-3837 ◽  
Author(s):  
Stephen R. Wecksler ◽  
Alexander Mikhailovsky ◽  
Dmitry Korystov ◽  
Peter C. Ford

1982 ◽  
Vol 37 (6) ◽  
pp. 744-747 ◽  
Author(s):  
Maliyakal E. John ◽  
Ralte Lalthantluanga ◽  
Gisela Liljeqvist ◽  
Sven Paléusa ◽  
Gerhard Braunitzer

Abstract The nitric oxide complex of hagfish hemoglobin exhibits electron spin resonance spectra centered around g = 2 with rhombic symmetry. The six coordinated spectrum is not influenced by protonation or presence of inositol hexaphosphate. Thus, the critical substitutions at E 7 (His → Gln) and E 11 (Yal → Ile) do not disrupt the proximal histidineiron bonds in the nitrosyl complex of this primitive hemoglobin, though the same type of substitution are known to cause destabilization of R quaternary structure in tetrameric mammalian nitrosylhemoglobins. This difference could be related to the difference in tension existing in the respective hemes of tetrameric and monomeric hemoglobins.


2013 ◽  
Vol 52 (6) ◽  
pp. 3207-3216 ◽  
Author(s):  
Ashley M. Wright ◽  
Homaira T. Zaman ◽  
Guang Wu ◽  
Trevor W. Hayton

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