Browsing by Subject "myoglobin"
Now showing items 1-5 of 5
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Article
Coupling of helix E-F motion with the O-nitrito and 2-nitrovinyl coordination in myoglobin
(2017)Myoglobin (Mb) is known to react slowly with nitirite to form the green pigment by NO2 − cordination to the heme Fe in the O-binding nitrito (O1[sbnd]N[dbnd]O2) mode and to the heme 2-vinyl position. Nitrite is a powerful ...
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Article
Nitrite coordination in myoglobin
(2017)The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional ...
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Article
Probing the nitrite and nitric oxide reductase activity of cbb3 oxidase: Resonance Raman detection of a six-coordinate ferrous heme-nitrosyl species in the binuclear b3/CuB center
(2015)In this work we report the first spectroscopic evidence demonstrating that cbb3 oxidase catalyzes the reduction of nitrite to nitrous oxide under reducing anaerobic conditions. The reaction proceeds through the formation ...
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Article
Resonance Raman detection of the myoglobin nitrito heme Fe-O-N=O/2-nitrovinyl species: Implications for helix E-helix F interactions
(2015)The description of biological activity in heme proteins responsible for activating small molecules requires identification of ligand movement into the metal and non-metal binding sites. Mechanisms of nitrite reductase ...
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Article
The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy
(2015)Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a3-nitro species in ba3-oxidase by resonance Raman spectroscopy. This provides the first ...