Nv. Karapetyan et al., Energy exchange between the chlorophyll antennae of monomeric subunits within the Photosystem I trimeric complex of the cyanobacterium Spirulina, PHOTOSYN R, 61(3), 1999, pp. 291-301
The energy exchange between antenna chlorophylls of the monomeric subunits
within a Photosystem I trimeric complex of the cyanobacterium Spirulina was
studied, comparing the kinetics of the light-induced decrease of Photosyst
em I fluorescence at 760 nm, emitted by the longwave chlorophyll absorbing
at 735 nm and P700 photooxidation. Both kinetics have been measured at 77 K
simultaneously using a fiberoptic system. The light-induced decrease of fl
uorescence at 760 nm in trimers was faster than P700 oxidation, although th
e decrease of fluorescence at 760 nm was ascribed to the quenching effect o
f oxidized P700 that is a stronger quencher of fluorescence at 760 nm than
P700 reduced [Shubin et al. (1995) J Photochem. Photobiol 27B: 153-160]. Th
e proportionality of the reciprocal value of the half time for the fluoresc
ence decrease at 760 nm in trimers to the light intensity indicates the pho
tochemical nature of the fluorescence quenching. The nonlinear relationship
between the variable part of fluorescence at 760 nm and the fraction of re
duced P700 is considered to be a result of an energetic connectivity of the
antennae of monomeric subunits within a trimer. When one P700 in PS I trim
ers of Spirulina is oxidized, the energy from an antenna of monomeric subun
it(s) with reduced P700 may migrate to a subunit with oxidized P700 and que
nched there. This may explain the slower rate of P700 photooxidation in tri
mers as compared with monomers. The analytical description of cooperativity
processes in Photosystem I coincides well with the measured data. A model
is presented describing the energetic interaction of chlorophyll antennae o
f monomeric subunits within the trimer via the extreme long-wavelength chlo
rophyll form. This intersubunit interaction may stimulate the dissipation o
f excess energy as heat and, therefore, protect the pigment-protein complex
against photodestruction.