NDLI: The relationship between different spectral forms of the protochlorophyllide oxidoreductase complex and the structural organisation of prolamellar bodies isolated from Zea mays

Content Provider	Springer Nature Link
Author	Selstam, Eva Brain, Anthony P. R. Williams, W. Patrick
Copyright Year	2011
Abstract	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 $_{650}$.
Starting Page	47
Ending Page	59
Page Count	13
File Format	PDF
ISSN	01668595
Journal	Photosynthesis Research
Volume Number	108
Issue Number	1
e-ISSN	15735079
Language	English
Publisher	Springer Netherlands
Publisher Date	2011-04-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Protochlorophyllide oxidoreductase Prolamellar body Protochlorophyllide Chlorophyllide Cubic membrane Plant Genetics & Genomics Plant Physiology Biochemistry Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science Medicine Biochemistry

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