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Interactions in Plastocyanin−Lysine Peptide and Related Systems
Author(s) -
Hirota Shun,
Yamauchi Osamu
Publication year - 2002
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/1099-0682(20021)2002:1<17::aid-ejic17>3.0.co;2-q
Subject(s) - plastocyanin , chemistry , peptide , lysine , cytochrome c , electron transfer , protein structure , copper protein , cytochrome , protein–protein interaction , biophysics , biochemistry , copper , enzyme , photochemistry , amino acid , organic chemistry , photosystem i , chloroplast , gene , biology , mitochondrion
The structure−function relationship of proteins is one of the major topics of protein studies. In spite of the importance of intermolecular interactions between proteins, which could control their functions, there are only a limited number of detailed studies on the protein structural changes induced by interaction with a protein or a peptide, because the associated changes in properties are small. Charged peptides, however, may be useful for studying the molecular recognition character of proteins and their interaction‐induced structural changes, since they do not have any visible absorption. The active site Cu of plastocyanin (PC) exhibited a longer Cu−S(Cys) bond length and a higher redox potential on binding of a lysine peptide, suggesting that lysine peptides induce a structural change in PC to adapt the copper site for facile electron transfer. Structural changes were also observed for cytochrome (cyt) f , cyt c , and cytochrome c peroxidase on interaction with charged peptides.