title: Photosynthetic activity of far-red light in green plants.
abstract: We have found that long-wavelength quanta up to 780 nm support oxygen evolution from the leaves of sunflower and bean. The far-red light excitations are supporting the photochemical activity of photosystem II, as is indicated by the increased chlorophyll fluorescence in response to the reduction of the photosystem II primary electron acceptor, Q(A). The results also demonstrate that the far-red photosystem II excitations are susceptible to non-photochemical quenching, although less than the red excitations. Uphill activation energies of 9.8+/-0.5 kJ mol(-1) and 12.5+/-0.7 kJ mol(-1) have been revealed in sunflower leaves for the 716 and 740 nm illumination, respectively, from the temperature dependencies of quantum yields, comparable to the corresponding energy gaps of 8.8 and 14.3 kJ mol(-1) between the 716 and 680 nm, and the 740 and 680 nm light quanta. Similarly, the non-photochemical quenching of far-red excitations is facilitated by temperature confirming thermal activation of the far-red quanta to the photosystem II core. The observations are discussed in terms of as yet undisclosed far-red forms of chlorophyll in the photosystem II antenna, reversed (uphill) spill-over of excitation from photosystem I antenna to the photosystem II antenna, as well as absorption from thermally populated vibrational sub-levels of photosystem II chlorophylls in the ground electronic state. From these three interpretations, our analysis favours the first one, i.e., the presence in intact plant leaves of a small number of far-red chlorophylls of photosystem II. Based on analogy with the well-known far-red spectral forms in photosystem I, it is likely that some kind of strongly coupled chlorophyll dimers/aggregates are involved. The similarity of the result for sunflower and bean proves that both the extreme long-wavelength oxygen evolution and the local quantum yield maximum are general properties of the plants.
authors.affiliation: Institute of Molecular and Cell Biology, University of Tartu, Riia Street 23, Tartu 51010, Estonia.
authors.forename: Hugo
authors.initials: H
authors.lastname: Pettai
authors.forename: Vello
authors.initials: V
authors.lastname: Oja
authors.forename: Arvi
authors.initials: A
authors.lastname: Freiberg
authors.forename: Agu
authors.initials: A
authors.lastname: Laisk
mesh_terms: D004579:Electron Transport; D006368:Helianthus / Q000378:metabolism*; D008027:Light; D010100:Oxygen / Q000378:metabolism; D027805:Phaseolus / Q000378:metabolism*; D010788:Photosynthesis / Q000502:physiology*; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex / Q000378:metabolism; D045332:Photosystem II Protein Complex / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
chemical_list: D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045332:Photosystem II Protein Complex; D010100:Oxygen