Visible-light induced hydrogen production using a polypeptide-chlorophyll complex with alpha-helix conformation.
Hydrogen production was accomplished under visible-light irradiation by using a system consisting of a biomolecule (chlorophyll a), methylviologen, ethylenediaminetetraacetic acid disodium salt and Pt-loaded poly(l-glutamate) (Poly(Glu)), in aqueous decylammonium chloride (DeAC) solution. Spectroscopic studies revealed that chlorophyll a is solubilized in the hydrophobic clusters of Pt-loaded Poly(Glu)-decylammonium chloride. In the Poly(Glu)-DeAC complex, the electron transfer occurred between chlorophyll a and methylviologen leading to hydrogen production. The most noticeable result is that the rate of hydrogen evolution depends on the change from the random coil to the alpha-helix in conformation of Poly(Glu) induced by the cooperative binding with DeAC.
Ngweniform
Pascaline
P
Department of Chemistry and BioScience, Faculty of Science, Kagoshima University, 1-21-35 Korimoto, Kagoshima, 890-0065, Japan.
Kusumoto
Yoshihumi
Y
Teshima
Takeo
T
Ikeda
Miyuki
M
Somekawa
Shouichi
S
Ahmmad
Bashir
B
D000588:Amines / Q000737:chemistry; D002942:Circular Dichroism; D004579:Electron Transport; D006859:Hydrogen / Q000737:chemistry / Q000528:radiation effects*; D057927:Hydrophobic and Hydrophilic Interactions; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000528:radiation effects*; D010777:Photochemistry; D010984:Platinum / Q000737:chemistry / Q000528:radiation effects; D011099:Polyglutamic Acid / Q000737:chemistry / Q000528:radiation effects*; D017433:Protein Structure, Secondary / Q000528:radiation effects; D012680:Sensitivity and Specificity; D012995:Solubility; D012996:Solutions / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014867:Water / Q000737:chemistry
D000588:Amines; D045342:Light-Harvesting Protein Complexes; D012996:Solutions; D014867:Water; D011099:Polyglutamic Acid; D010984:Platinum; D006859:Hydrogen; C004744:decylamine