Browsing by Subject "Cytochrome b Group"
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
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 ...
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Article
Time-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: Implications for O2 input and H 2O/H+ output channels
(2004)We have applied FTIR and time-resolved step-scan Fourier transform infrared (TRS2-FTIR) spectroscopy to investigate the dynamics of the heme-CuB binuclear center and the protein dynamics of mammalian aa3, Pseudomonas ...