Superoxide Dismutase Activity of the Naturally Occurring Human Serum Albumin–Copper Complex without Hydroxyl Radical Formation |
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| Authors: | Ryunosuke Kato Dr Matofusa Akiyama Prof?Dr Hiroyoshi Kawakami Prof?Dr Teruyuki Komatsu |
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| Affiliation: | 1. 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;2. Department of Applied Chemistry, Tokyo Metropolitan University, 1‐1 Minami‐Osawa, Hachioji‐shi, Tokyo 192‐0397 (Japan) |
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| Abstract: | 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 CuII 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 MnIII‐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. |
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| Keywords: | copper complex enzymes human serum albumin proteins superoxide dismutase |
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