NDLI: Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II

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Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions

Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II

Conformational changes and their role in non-radiative energy dissipation in photosystem II reaction centres

Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine

Solving the structure of plant photosystem I—biochemistry is vital

Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy

The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides

Isolation and characterization of a xanthophyll-rich fraction from the thylakoid membrane of Dunaliella salina(green algae)

The mechanism for dioxygen formation in PSII studied by quantum chemical methods

A role of the C-terminal extension of the photosystem II D1 protein in sensitivity of the cyanobacterium Synechocystis PCC 6803 to photoinhibition

The role of D1-Ala344 in charge stabilization and recombination in Photosystem II

Kinetic characterisation of the light-driven protochlorophyllide oxidoreductase (POR) from Thermosynechococcus elongatus

The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

Degradation of the main Photosystem II light-harvesting complex

Functional flexibility and acclimation of the thylakoid membrane

Granal stacking of thylakoid membranes in higher plant chloroplasts: the physicochemical forces at work and the functional consequences that ensue

Photosystem I: a search for green plant trimers

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Photochemical & Photobiological Sciences Vol - 4 Issue - 9

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Photochemical & Photobiological Sciences Vol -2

Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II

Content Provider	Royal Society of Chemistry (RSC)
Author	Ananyev, Gennady Nguyen, Tuan Dismukes, G. Charles Putnam-Evans, Cindy
Copyright Year	2005
Abstract	The chlorophyll-binding protein CP43 is an inner subunit of the Photosystem II (PSII) reaction center core complex of all oxygenic photoautotrophs. X-Ray structural evidence places the guanidinium cation of the conserved arginine 357 residue of CP43 within a few Ångstroms to the Mn4Ca cluster of the water-oxidizing complex (WOC) and has been implicated as a possible carbonate binding site. To test the hypothesis, the serine mutant, CP43-R357S, from Synechocystis PCC 6803 was investigated by PSII variable fluorescence (Fv/Fm) and simultaneous flash O2 yield measurements in cells and thylakoid membranes. The R357S mutant assembles PSII-WOC centers, but is unable to grow photoautotrophically. Reconstitution of O2 evolution by photoactivation and the occurrence of period-four oscillations of Fv/Fm establishes that the R357S mutant contains an assembled Mn4Ca cluster, but turnover is impaired as seen by an 11-fold larger Kok double miss parameter and faster decay of upper S states. Using pulsed light to avoid photoinactivation, wild-type cells and thylakoid membranes exhibit a 2–4-fold loss in O2 evolution rate upon partial bicarbonate depletion under multiple turnover conditions, while the R357S mutant is unaffected by bicarbonate. Arginine R357 appears to function in binding a (bi)carbonate ion essential to normal catalytic turnover of the WOC. The quantum yield of electron donation from the WOC into PSII increases with decreasing turnover rate in R357S mutant cells and involves an aborted two-flash pathway that is distinct from the classical four-flash pattern. We speculate that an altered photochemical mechanism for O2 production occurs via formation of hydrogen peroxide, by analogy to other treatments that retard the kinetics of proton release into the lumen.
Starting Page	991
Ending Page	998
Page Count	8
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	4
Issue Number	12
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/b507519j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Phototroph Oxygen Hydrogen peroxide PSII Kok Guanidine Serine Fluorescence Ion WOC Photosystem II Synechocystis Thylakoid Protein Quantum tunnelling Bicarbonate Classical physics Arginine Photoswitch Proton Mutation Photochemistry
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II

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Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II