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The relationship between different spectral forms of the protochlorophyllide oxidoreductase complex and the structural organisation of prolamellar bodies isolated from Zea mays
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). (Eva Selstam)
2011 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 108, no 1, 47-59 p.Article in journal (Refereed) Published
Abstract [en]

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 650 nm (POR-PChlide ( 640/650 )), and a non-photoconvertible form, with absorption maxima at 635 nm (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 ).

Place, publisher, year, edition, pages
2011. Vol. 108, no 1, 47-59 p.
Keyword [en]
protochlorophyllide oxidoreductase, prolamellar body, protochlorophyllide, chlorophyllide, cubic membrane
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URN: urn:nbn:se:umu:diva-44329DOI: 10.1007/s11120-011-9653-1PubMedID: 21505944OAI: diva2:420174
Available from: 2011-05-31 Created: 2011-05-31 Last updated: 2011-06-07Bibliographically approved

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