Bovine serum albumin coordinated iron-sulfur cluster as a hydrogenase model.
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概要
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The bovine serum albumin coordinated Fe<SUB>4</SUB>S<SUB>4</SUB>-cluster, which had hydrogenase activity, was synthesized. Its physical and chemical characteristics were then compared with those of natural hydrogenase. Though the affinities of hydrogenase and the albumin-coordinated Fe<SUB>4</SUB>S<SUB>4</SUB>-cluster for the substrate, methyl viologen, were similar, the hydrogenase activity for hydrogen evolution was 10<SUP>5</SUP> times greater than the cluster. Two types of Fe<SUB>4</SUB>S<SUB>4</SUB>-clusters, coordinated by the fragments of the cleaved albumin obtained by treatment with cyanogen bromide, were synthesized, and their hydrogenase activities were compared. The activity with the iron-sulfur cluster incorporated in the fragment with MW 40000 was much higher than that of the one incorporated in the fragment with MW 20000. The amino acid arrangement to form the active site was discussed on the analogy of the other iron-sulfur proteins.
- 公益社団法人 日本化学会の論文
著者
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Okura Ichiro
Department Of Bioengineering Tokyo Institute Of Technology
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Kobayashi Masatoshi
Department Of Anatomy & Histology Kurume University School Of Medicine
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Nakamura Satoshi
Department Of Acoustic And Speech Research Advance Telecommunications Research Institute International
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Kobayashi Masatoshi
Department of Chemical Engineering, Tokyo Institute of Technology
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Okura Ichiro
Department of Chemical Engineering, Tokyo Institute of Technology
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