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Diiron Dithiolate Complex Induced Helical Structure of Histone and Application in Photochemical Hydrogen Generation
journal contribution
posted on 2019-05-22, 00:00 authored by Xiantao Hu, Weijian Chen, Shuyi Li, Jian Sun, Ke Du, Qiuyu Xia, Fude FengVery-lysine-rich
calf thymus histone proteins form disordered structure
and hydrophobic interaction-driven aggregates in weakly acidic solution.
We reported that the conjugation of diiron dithiolate complex to the
lysine residues induced formation of helical conformation and condensed
nanoassemblies with a high loading capacity up to 18.7 wt %. The incorporated
diiron dithiolate complex showed photocatalytic activity for hydrogen
evolution in aqueous solutions, with a turnover number (based on [FeFe]
catalyst moiety) up to 359 that was more than 6 times that of the
free catalyst. The increase of helical conformation in proteins was
well correlated to the increasing enhancement of photocatalytic activity.
We demonstrated that the [FeFe]–hydrogenase-mimic biohybrid
system based on the photocatalyst-induced protein conformational conversion
and reassembly is efficient for hydrogen generation regardless of
the relatively large size.