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1.
Phys Chem Chem Phys ; 12(40): 12973-7, 2010 Oct 28.
Article in English | MEDLINE | ID: mdl-20820569

ABSTRACT

For dye-sensitized solar-cell devices fabricated from porphyrin sensitizers with links of varied length (PE1-PE4) adsorbed on anodic titanium-oxide nanotube arrays, we measured induced photocurrent and photovoltage decays under constant bias illumination; the evaluated efficiencies of charge collection of the devices show a systematic trend PE4 > PE3 > PE2 > PE1 at a large short-circuit current, implying that a long link would improve the charge separation if the electrons were effectively injected into the semiconductor.

2.
J Phys Chem B ; 114(12): 4327-34, 2010 Apr 01.
Article in English | MEDLINE | ID: mdl-20201495

ABSTRACT

Intramolecular binding of a ligand with an alkyl link, (-CH(2))(3), covalently bound to a residue near the active site of the protein forms a novel steroid-sensing model. A genetically engineered big up tri, open(5)-3-ketosteroid isomerase (KSI) was designed to conjugate uniquely with this ligand at its Cys-86 through the formation of a disulfide bond. The steady-state protein-ligand binding, mediated by hydrophobic interactions, was confirmed with fluorescence spectra, and the fluorophore-labeled peptide sequence was identified with tandem mass spectra. A comparison of steady-state fluorescence spectra of various fluorophore-labeled KSI mutants reveals that the emission characteristics vary with environmental factors. An evaluation of the decay of the fluorescence anisotropy of the fluorophore indicates the existence of an intramolecular protein-ligand binding interaction. The measurement of time-resolved fluorescence anisotropy of various protein-ligand complexes yielded values of anisotropy decay representing the degrees of freedom of the fluorophore related to its location, inside or outside the steroid-binding domain. When 19-norandrostenedione (19-NA) was added to this protein-ligand system, competitive binding between the ligand and the steroid was observed; this finding confirms the feasibility of the design of steroid detection with engineered KSI. On integration of this protein-ligand system with a silicon-based nanodevice (a p-type field-effect transistor with an ultrathin body), a noncharged steroid, 19-NA, became detectable at a micromolar level ( Biosens. Bioelectron. 2008 , 23 , 1883 ).


Subject(s)
Fluorescence Polarization , Models, Theoretical , Proteins/chemistry , Steroids/analysis , Tandem Mass Spectrometry
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