Browsing by Subject "cytochrome b"
Now showing items 1-5 of 5
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Article
Detection of the His-heme Fe2+-NO species in the reduction of NO to N2O by ba3-oxidase from thermus thermophilus
(2005)Reaction pathways in the enzymatic formation and cleavage of the N-N and N-O bonds, respectively, are difficult to verify without the structure of the intermediates, but we now have such information on the heme a3 2+-NO ...
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Article
Nitric oxide activation and reduction by heme-copper oxidoreductases and nitric oxide reductase
(2008)The understanding of the dynamics and conformational control involved in the interplay between structure and function of nitric oxide reductase (Nor) and heme-copper oxidoreductases in their function to convert nitric oxide ...
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Article
Observation of the equilibrium CuB-CO complex and functional implications of the transient heme a3 propionates in cytochrome ba3-CO from Thermus thermophilus. Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studies
(2002)We report the first evidence for the existence of the equilibrium CuB 1+-CO species of CO-bound reduced cytochrome ba3 from Thermus thermophilus at room temperature. The frequency of the C-O stretching mode of CuB 1+-CO ...
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Article
Resonance Raman detection of the Fe2+-C-N modes in heme-copper oxidases: A probe of the active site
(2004)Resonance Raman spectroscopy has been employed to investigate the reduced cyano complexes of cytochrome aa3 from bovine heart and Rhodobacter sphaeroides and of cytochrome bo3 from E. coli. In the aa 3-type oxidases, the ...
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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 ...