منابع مشابه
Carbon monoxide-driven reduction of ferric heme and heme proteins.
Oxidized cytochrome c oxidase in a carbon monoxide atmosphere slowly becomes reduced as shown by changes in its visible spectra and its reactivity toward oxygen. The "auto-reduction" of cytochrome c oxidase by this procedure has been used to prepare mixed valence hybrids. We have found that this process is a general phenomenon for oxygen-binding heme proteins, and even for isolated hemin in bas...
متن کاملHNO/NO Conversion Mechanisms of Cu-Based HNO Probes with Implications for Cu,Zn-SOD
HNO has broad biological effects and pharmacological activities. Direct HNO probes for in vivo applications were recently reported, which are CuII-based complexes having fluorescence reporters with reaction to HNO resulting in CuI systems and the release of NO. Their coordination environments are similar to that in Cu,Zn-superoxide dismutase (SOD), which plays a significant role in cellular HNO...
متن کاملFluoride binding to the cytochrome c ferric heme octapeptide. A model for anion binding to the active site of high spin ferric heme proteins.
The temperature dependence of the magnetic susceptibility of the ferric hemeoctapeptide from cytochrome c was measured in the presence and absence of fluoride ion to study the fluoride binding equilibrium of the hemeoctapeptide. The shift in the 1H NMR signal of sodium 4,4-dimethyl-4-silapentanesulfonate caused by the hemeoctapeptide was measured from -11 to 80 degrees C in a D2O/ethylene glyco...
متن کاملDirect ab initio dynamics studies of the reactions of HNO with H and OH radicals
Ab initio calculations using the UMP2 and UQCISD methods with correlation consistent double-zeta and triple-zeta basis sets were applied to study the reactions of HNO with H and OH radicals. The classical energy barrier for the abstraction H+HNO!H2 +NO is 0.5 kcal/mol. The reaction path of OH+HNO is: OH+HNO!HNO(OH)-complex!TS!NO(H2O)complex!H2O+NO with no energy barrier relative to OH+HNO entra...
متن کاملOver or under: hydride attack at the metal versus the coordinated nitrosyl ligand in ferric nitrosyl porphyrins.
Hydride attack at a ferric heme-NO to give an Fe-HNO intermediate is a key step in the global N-cycle. We demonstrate differential reactivity when six- and five-coordinate ferric heme-NO models react with hydride. Although Fe-HNO formation is thermodynamically favored from this reaction, Fe-H formation is kinetically favored for the 5C case.
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2018
ISSN: 1433-7851,1521-3773
DOI: 10.1002/anie.201807699