期刊
CHEMPHYSCHEM
卷 10, 期 1, 页码 144-150出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.200800536
关键词
enzyme catalysis; photophysics; porphyrins; transient absorption spectroscopy; UV/Vis spectroscopy
资金
- Forschungsgemeinschaft [HE 2657/2-1, PO 563/9-1]
- Integrated Initiative of Infrastructure project LASERLAB-EUROPE [RII3-CT-2003-506350]
- Fonds der Chemischen Industrie
The photochemistry of protochlorophyllide a, a precursor in the biosynthesis of chlorophyll and substrate of the light regulated enzyme protochlorophyllide oxidoreductase, is investigated by pump-probe spectroscopy. Upon excitation into the lowest lying Q-band the light induced changes ore recorded over a wide range of probe wavelengths in the visible and near-IR region between 500 and 1000 nm. Following excitation, an initial ultrafast 450 Is process is observed related to the motion out of the Franck-Condon region on the excited state surface; thus directly unraveling previous suggestions based on time-resolved fluorescence measurements (ChemPhysChem 2006, 7, 1727-1733). Furthermore, the data reveals a previously concealed photointermediate, whose formation on a nanosecond timescale matches the overall fluorescence decay and is assigned to a triplet state. The implications of this finding with respect to the photochemistry of NADPH.-protochlorophyllide oxidoreductase (POR) ore discussed.
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