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Rapid binding of copper(I) to folded aporusticyanin
Author(s) -
Alcaraz Luis A.,
Donaire Antonio
Publication year - 2005
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.2005.08.048
Subject(s) - copper , chemistry , folding (dsp implementation) , kinetics , copper protein , biophysics , crystallography , protein folding , biochemistry , biology , organic chemistry , physics , quantum mechanics , electrical engineering , engineering
Kinetics of copper uptake in both oxidation states by the folded and unfolded forms of the type 1 copper protein rusticyanin have been studied. The speed of the binding of copper(I) to the folded rusticyanin is fast, and of the same order of magnitude as copper(I) uptake by the unfolded form. Thus, the binding of copper can be subsequent to the protein folding, contrary to previous proposals. Implications for the mechanism of the formation of the active holoprotein in vivo are discussed.