Fluorescence spectroscopy of the longwave chlorophylls in trimeric and monomeric photosystem I core complexes from the cyanobacterium Spirulina platensis.
The organization and interaction of chlorophylls (Chl) and the kinetics of the energy transfer in the core antenna of photosystem I (PSI) trimeric and monomeric complexes, isolated from Spirulina platensis with Triton X-100 have been studied by stationary and time-resolved fluorescence. At 295 K both complexes show an unusually intense long-wavelength emission band with prominent peaks at 730 nm (trimers) or 715 nm (monomers), whose intensity is independent of the redox state of P700. A broad band extending from 710 to 740 nm in the absorption and fluorescence excitation spectra of trimers also indicates the existence of the longwave Chls at 295 K. The 77 K fluorescence emission of PSI trimers frozen after addition of dithionite under illumination (P700 and the PSI acceptor side reduced) shows an intense band at 760 (F760) and a smaller one at 725 nm (F725); when P700 is oxidized, the intensity of F760 decreases about 15 times. In the 77 K spectrum of monomers only F725 is present in the longwave region, and its intensity does not depend on the redox state of P700. Bands of Chls with maxima near 680, 710, and 738 nm were found in the 77 K excitation spectrum of trimers, and bands near 680 and 710 nm were seen in the spectrum of monomers. Five spectrally different red Chl forms in PSI trimers and three red Chl in monomers have been resolved by deconvolution of their 77 K absorption spectra. The difference absorption spectrum, trimers-minus-monomers, shows that the appearance of the 735 nm band in trimers is accompanied by a decrease of 708, 698, and 688 nm bands present in monomers. The reversible changes of F760 intensity of Spirulina membranes as a result of their salt treatment confirm the idea that the most longwave Chl form originates from an interaction of Chls bound to different monomeric PSI subunits forming the trimer. The time-resolved fluorescence spectra of PSI trimers and monomers, measured at 287 K in the region 680-770 nm, are substantially different, although a set of similar lifetimes (9, approximately 30, approximately 66, and 1400-2200 ps) was necessary for a good fit. No effect of P700 redox state was observed on the fluorescence kinetics of both complexes at 287 K.
Karapetyan
N V
NV
Max-Planck-Institut für Strahlenchemie, Ruhr, Germany.
Dorra
D
D
Schweitzer
G
G
Bezsmertnaya
I N
IN
Holzwarth
A R
AR
D002734:Chlorophyll / Q000737:chemistry* / Q000378:metabolism; D000458:Cyanobacteria / Q000737:chemistry* / Q000378:metabolism; D004735:Energy Transfer; D007700:Kinetics; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll