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Interaction of bicarbonate with the manganese-stabilizing protein of photosystem II

Paper ID Volume ID Publish Year Pages File Format Full-Text
30992 44524 2010 8 PDF Available
Title
Interaction of bicarbonate with the manganese-stabilizing protein of photosystem II
Abstract

The effect of reversible removal of HCO3- on structural re-arrangements in the Mn-stabilizing protein (MSP) of photosystem II, isolated from pea leaves, was studied using measurements of characteristic alterations in fluorescence of hydrophobic probe 8-anilino-1-naphthalene-sulfonic acid (ANS). It was shown that the treatments capable of removal of HCO3- (or CO2) from possible binding sites in MSP (pH lowering from 6.5 to 3.5, addition of a structurally similar anion HCO3- in concentration 1–20 mM or air evacuation at pH 3.5) result in a significant (up to 370%) increase of ANS fluorescence (indicative of structural changes in MSP), whereas HCO3- lowers the ANS fluorescence to the initial level observed in untreated protein at pH 6.5. Since the effects are revealed at (sub)micromolar concentrations of HCO3-, the specific high-affinity binding of HCO3- (or CO2) to MSP (required for its native structure preservation) is proposed. Possible bicarbonate binding sites and its physiological role within the water-oxidizing complex of photosystem II are discussed.

Keywords
Photosystem II; Bicarbonate; Manganese-stabilizing protein; 8-Anilino-1-naphthalene-sulfonic acid (ANS)
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Interaction of bicarbonate with the manganese-stabilizing protein of photosystem II
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 100, Issue 1, 2 July 2010, Pages 30–37
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us