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An examination of the basic blue copper protein from cucumber peelings by 1 H‐NMR
Author(s) -
King G.,
Andary T.A.,
Freeman H.C.,
Gavrilovic L.,
Wright P.E.
Publication year - 1984
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(84)80097-6
Subject(s) - copper protein , plastocyanin , azurin , copper , chemistry , bioinorganic chemistry , ligand (biochemistry) , crystallography , metalloprotein , nuclear magnetic resonance spectroscopy , amino acid , redox , titration , stereochemistry , inorganic chemistry , biochemistry , organic chemistry , enzyme , photosystem i , receptor , chloroplast , gene
The 1 H‐NMR spectrum of cucumber basic blue protein (CBP) has been recorded. Examination of the spectrum of the reduced protein suggests that one or more sidechains exist in conformations which interconvert slowly at ambient temperatures. His 39, His 84 and Met 89 are identified as copper ligands by redox titration and by amino acid sequence homology with plastocyanin and azurin. The importance of a Phe sidechain close to the Met ligand in the potential blue copper site is confirmed. Broadening of His ligand resonances at elevated temperatures reveals an exchange process at the reduced copper centre.