The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre.
A copper-containing domain of the caa3-type oxidase from Bacillus subtilis has been expressed as a water-soluble protein in the cytoplasm of Escherichia coli. Electron paramagnetic resonance (EPR) spectra of this purple domain show well-resolved lines in the gz resonance, both at X-band and S-band frequencies. Interpretation of EPR spectra and analytical data indicate a binuclear copper site consisting of one Cu2+ and one Cu1+. This copper site closely resembles CuA in subunit II of cytochrome c oxidase and is shown here to be a mixed-valence [Cu2+-Cu1+] binuclear centre.
von Wachenfeldt
C
C
Department of Molecular and Cellular Biology, BioCentrum Amsterdam, Vrije Universiteit, The Netherlands.
de Vries
S
S
van der Oost
J
J
D001412:Bacillus subtilis / Q000201:enzymology*; D001483:Base Sequence; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D017931:DNA Primers; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D055095:Optics and Photonics
D017931:DNA Primers; D007477:Ions; D003300:Copper; D003576:Electron Transport Complex IV