caa a22 4500 44589007X CHVBK 20180317145613.0 cr unu---uuuuu 170323e20110501xx s 000 0 eng 10.1007/s11120-011-9653-1 doi (NATIONALLICENCE)springer-10.1007/s11120-011-9653-1 The relationship between different spectral forms of the protochlorophyllide oxidoreductase complex and the structural organisation of prolamellar bodies isolated from Zea mays [Elektronische Daten] [Eva Selstam, Anthony Brain, W. Williams] Incubation of prolamellar bodies (PLB) in high-salt media leads to changes in PLB structure and properties of their protochlorophyllide oxidoreductase-protochlorophyllide (POR-PChlide) complex. The paracrystalline organisation typical of PLB is disrupted and NADPH dissociates from photoconvertible POR-PChlide, with absorption maxima at 640 and 650nm (POR-PChlide 640/650), and a non-photoconvertible form, with absorption maxima at 635nm (POR-PChlide 635), is formed. These effects are strongly dependent on the valence of the cation of the perturbing salt, indicating that they involve surface double layers effects. They are also influenced by the nature of the anion and by high concentrations of non-electrolytes, suggesting the involvement of surface hydration effects. The structural changes are largely, if not entirely, independent of the presence of excess NADPH. Changes to the POR-PChlide complex, however, are strongly inhibited by excess NADPH suggesting that the two sets of changes may not be causally linked. As long as the disruption is not too great, the structural changes seen on incubation of PLB in high salt media lacking excess NADPH are reversed on removal of the high salt perturbation. This reversal is independent of the presence or absence of added NADPH. Reformation of photoconvertible POR-PChlide, however, requires the presence of NADPH. The reformation of paracrystalline PLB in the absence of NADPH strongly indicates that preservation of PLB structure, in isolated PLB preparations at least, is independent of the presence or absence of POR-PChlide 650. Springer Science+Business Media B.V., 2011 Protochlorophyllide oxidoreductase nationallicence Prolamellar body nationallicence Protochlorophyllide nationallicence Chlorophyllide nationallicence Cubic membrane nationallicence Selstam Eva Umeå Plant Science Centre, Department of Plant Physiology, University of Umeå, Umeå, Sweden aut Brain Anthony Biochemistry Department, King's College, University of London, London, UK aut Williams W. Biochemistry Department, King's College, University of London, London, UK aut Photosynthesis Research Springer Netherlands 108/1(2011-05-01), 47-59 0166-8595 108:1<47 2011 108 11120 https://doi.org/10.1007/s11120-011-9653-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11120-011-9653-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Selstam Eva Umeå Plant Science Centre, Department of Plant Physiology, University of Umeå, Umeå, Sweden aut NATIONALLICENCE 700 1- Brain Anthony Biochemistry Department, King's College, University of London, London, UK aut NATIONALLICENCE 700 1- Williams W. Biochemistry Department, King's College, University of London, London, UK aut NATIONALLICENCE 773 0- Photosynthesis Research Springer Netherlands 108/1(2011-05-01), 47-59 0166-8595 108:1<47 2011 108 11120 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer