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HERO ID
2860987
Reference Type
Journal Article
Title
Properties of the indole ring in metal complexes. A comparison with the phenol ring
Author(s)
Shimazaki, Y; Yajima, T; Yamauchi, O
Year
2015
Is Peer Reviewed?
Yes
Journal
Journal of Inorganic Biochemistry
ISSN:
0162-0134
EISSN:
1873-3344
Language
English
PMID
25817198
DOI
10.1016/j.jinorgbio.2015.03.001
Abstract
Tryptophan (Trp), an essential amino acid, has an indole ring with a high electron density and is frequently seen at the proximal position of the metal site in metalloproteins. For example, the indole ring of Trp has been reported to interact weakly with Cu(I) in a Cu chaperone CusF. Another aromatic amino acid, tyrosine (Tyr), has a phenol ring, which is an important metal binding site in various metalloproteins. Although the structures of the aromatic rings are different, they both have a weakly acidic moiety and perform some similar roles in biological systems, such as radical formation and electron transfer. In this review, we focus on these and other properties of the indole and phenol rings in metal-containing systems.
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