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
Noor, M. R.
Google Scholar check
MetadataShow full item record
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 evidence for the structure of a nitrite-bound species in the binuclear heme/copper center of cytochrome c oxidases. © 2015 The Royal Society of Chemistry.
Showing items related by title, author, creator and subject.
Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus Pinakoulaki, Eftychia; Soulimane, T.; Varotsis, Constantinos (2002)Fourier transform infrared (FTIR) and step-scan time-resolved FTIR difference spectra are reported for the [carbonmonoxy]cytochrome caa3 from Thermus thermophilus. A major C-O mode of heme a3 at 1958 cm-1 and two minor ...
Time-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: Implications for O2 input and H 2O/H+ output channels Koutsoupakis, Constantinos; Pinakoulaki, Eftychia; Stavrakis, Stavros; Daskalakis, Vangelis; Varotsis, Constantinos (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 ...
Nikolopoulos, Georgios K.; Tsiodras, Sotirios; Bonovas, Stefanos; Hatzakis, A. (2012)Infection with Human Immunodeficiency Virus (HIV) remains a global public health problem. Although the epidemic has not been completely controlled, there was considerable progress in HIV prevention and treatment during the ...