title: Charge recombination reactions in photosystem II. 2. Transient absorbance difference spectra and their temperature dependence.
abstract: Absorbance difference spectra of the transient states in photosystem II (PS II) have been examined in the Qv absorption region between 660 and 700 nm. The P680+Pheo-/P680Pheo, 3P680/P680, and P680+QA-/P680QA spectra were measured in O2-evolving PS II core complexes from Synechococcus and PS II-enriched membrane fragments from spinach. The low-temperature absorbance difference spectra vary only slightly between both PS II preparations. The 3P680/P680 spectrum is characterized by a bleaching at 685 nm at 25 K and indicates weak exciton coupling with neighboring pigment(s). We conclude that P680 absorbs at 685 nm in more intact PS II preparations at cryogenic temperature. The difference spectra of the radical pairs are strongly temperature dependent. At low temperature the P680+QA-/P680QA- spectrum exhibits the strongest bleaching at 675 nm whereas the P680+Phe-/P680Pheo spectra show two distinct bleaching bands at 674 and 684 nm. It is suggested that an electrochronic red shift resulting in a bleaching at 675 nm and an absorbance increase at about 682 nm dominates the spectral features of the charge-separated states. On the basis of the present results and those in the literature, we conclude that the interactions between the pigments and especially the organization of the primary donor must be quite different in PS II compared to bacterial reaction centers, although the basic structural arrangement of the pigments might be similar. Spectral data obtained with samples in the presence of singly and doubly reduced QA indicate that the primary photochemistry in PS II is not strongly influenced by the redox state of QA at low temperature and confirm the results of the accompanying paper [Van Mieghem, F. J. E., Brettel, K., Hillmann, B., Kamlowski, A., Rutherford, A. W., & Schlodder, E. (1995) Biochemistry 34, 4798-4813]. The spectra of the primary radical pair and the reaction center triplet obtained with more intact PS II preparations differ widely from those of D1/D2/cyt b-559 complexes. In the latter sample, where 3P680 formation results in a bleaching at 680 nm, the P680+Pheo-/P680Pheo spectrum shows only one broad bleaching band at about 680 nm, and the main bleaching due to photoaccumulation of Pheo- at 77 K appears at 682 nm instead of 685 nm in PS II core complexes. This indicates that the removal of the core antenna which is accompanied by the loss of QA causes also structural changes of the reaction center.
authors.affiliation: Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität Berlin, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Hillmann
authors.forename: K
authors.initials: K
authors.lastname: Brettel
authors.forename: F
authors.initials: F
authors.lastname: van Mieghem
authors.forename: A
authors.initials: A
authors.lastname: Kamlowski
authors.forename: A W
authors.initials: AW
authors.lastname: Rutherford
authors.forename: E
authors.initials: E
authors.lastname: Schlodder
mesh_terms: D000458:Cyanobacteria / Q000737:chemistry*; D005609:Free Radicals; D007700:Kinetics; D010084:Oxidation-Reduction; D010777:Photochemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D013057:Spectrum Analysis; D013696:Temperature
chemical_list: D005609:Free Radicals; D045322:Photosynthetic Reaction Center Complex Proteins