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Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze‐quench EPR study
Author(s) -
Bennett Brian,
Hill Bruce C.
Publication year - 2011
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/j.febslet.2011.02.014
Subject(s) - electron paramagnetic resonance , chemistry , nuclear magnetic resonance , physics
The Bacillus subtilis version of SCO1 (BsSCO) is required for assembly of Cu A in cytochrome c oxidase and may function in thiol‐disulfide exchange and/or copper delivery. BsSCO binds Cu(II) with ligation by two cysteines, one histidine and one water. However, copper is a catalyst of cysteine oxidation and BsSCO must avoid this reaction to remain functional. Time resolved, rapid freeze‐quench (RFQ) electron paramagnetic resonance of apo‐BsSCO reacting with Cu(II) reveals an initial Cu(II) species with two equatorially coordinated nitrogen atoms, but no sulfur. We propose that BsSCO evolves from this initial sulfur free coordination of Cu(II) to the final dithiolate species via a change in conformation, and that the initial binding by nitrogen is a means for BsSCO to avoid premature thiol oxidation.