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The Cu A site of the caa 3 ‐type oxidase of Bacillus subtilis is a mixed‐valence binuclear copper centre
Author(s) -
von Wachenfeldt Claes,
de Vries Simon,
van der Oost John
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80182-7
Subject(s) - bacillus subtilis , copper , valence (chemistry) , chemistry , oxidase test , crystallography , biochemistry , biology , enzyme , genetics , bacteria , organic chemistry
A copper‐containing domain of the caa 3 ‐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 g z resonance, both at X‐band and S‐band frequencies. Interpretation of EPR spectra and analytical data indicate a binuclear copper site consisting of one Cu 2+ and one Cu 1+ . This copper site closely resembles Cu A in subunit II of cytochrome c oxidase and is shown here to be a mixed‐valence [Cu 2+ ‐Cu 1+ ) binuclear centre.