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Superoxide Dismutase Activity of the Naturally Occurring Human Serum Albumin–Copper Complex without Hydroxyl Radical Formation
Author(s) -
Kato Ryunosuke,
Akiyama Matofusa,
Kawakami Hiroyoshi,
Komatsu Teruyuki
Publication year - 2014
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201301285
Subject(s) - chemistry , superoxide dismutase , human serum albumin , hydroxyl radical , superoxide , copper , reactive oxygen species , serum albumin , albumin , porphyrin , oxygen , biochemistry , radical , medicinal chemistry , enzyme , organic chemistry
The superoxide radical anion (O 2 .− ) is biologically toxic and contributes to the pathogenesis of various diseases. Here we describe the superoxide dismutase (SOD) activity of human serum albumin (HSA) complexed with a single Cu II ion at the N‐terminal end (HSA–Cu complex). The structure of this naturally occurring copper‐coordinated blood serum protein has been characterized by several physicochemical measurements. The O 2 .− dismutation ability of the HSA–Cu (1:1) complex is almost the same as that of the well‐known SOD mimics, such as Mn III ‐tetrakis( N ‐methylpyridinium)porphyrin. Interestingly, the HSA–Cu complex does not induce a subsequent Fenton reaction to produce the hydroxyl radical (OH . ), which is one of the most harmful reactive oxygen species .