Superoxide dismutase activity of the naturally occurring human serum albumin-copper complex without hydroxyl radical formation.
The superoxide radical anion (O2(.-)) 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 O2(.-) 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.
Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551 (Japan), Fax: (+81) 3-3817-1910.
Ryunosuke
R
Kato
Matofusa
M
Akiyama
Hiroyoshi
H
Kawakami
Teruyuki
T
Komatsu
D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D006801:Humans; D017665:Hydroxyl Radical; D008958:Models, Molecular; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000737:chemistry / Q000378:metabolism*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000378:metabolism*
D009942:Organometallic Compounds; D012709:Serum Albumin; D017665:Hydroxyl Radical; D003300:Copper; D013482:Superoxide Dismutase
copper complex; enzymes; human serum albumin; proteins; superoxide dismutase