Carbonic Anhydrase Activity of the Photosystem II OEC33 Protein from Pea

Lu, Yih-Kuang; Theg, Steven M.; Stemler, Alan

doi:10.1093/pcp/pci209

Cited by 33 publications

(24 citation statements)

References 35 publications

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“…S4). Mn 2ϩ binding to PsbO has indeed been demonstrated previously in isolated PsbO from higher plants (72)(73)(74). As in the present study and Ref.…”

Section: Quantification Of the Relative Concentrations Of Ps Ii-boundsupporting

confidence: 89%

See 1 more Smart Citation

The Basic Properties of the Electronic Structure of the Oxygen-evolving Complex of Photosystem II Are Not Perturbed by Ca2+ Removal

Lohmiller¹,

Cox²,

Su³

et al. 2012

Journal of Biological Chemistry

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“…S4). Mn 2ϩ binding to PsbO has indeed been demonstrated previously in isolated PsbO from higher plants (72)(73)(74). As in the present study and Ref.…”

Section: Quantification Of the Relative Concentrations Of Ps Ii-boundsupporting

confidence: 89%

“…51, protein-bound Mn 2ϩ did not show a CW EPR signal, but a six-line signal was observed after denaturation of the protein (73). PsbO was reported to show carbonic anhydrase activity, which was maximal in the presence of Mn 2ϩ (74 here (see supplemental data and Ref. 61).…”

Section: Quantification Of the Relative Concentrations Of Ps Ii-boundmentioning

confidence: 65%

The Basic Properties of the Electronic Structure of the Oxygen-evolving Complex of Photosystem II Are Not Perturbed by Ca2+ Removal

Lohmiller¹,

Cox²,

Su³

et al. 2012

Journal of Biological Chemistry

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“…A low level of carbonic anhydrase (CA) activity, more than 10 3 slower than typical Zn 2+ -CA, has been found to be intrinsic to oxygenevolving PS II membranes [69,70]. A soluble CA activity was found associated with the 33 kDa extrinsic protein of PS II (PsbO) and depends on the concentration of Mn 2+ and Cl − .…”

Section: Bicarbonate Ion-bicarbonatementioning

confidence: 99%

Photoassembly of the water-oxidizing complex in photosystem II

Dasgupta

Ananyev

Dismukes

2008

Coordination Chemistry Reviews

167

121

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The light-driven steps in the biogenesis and repair of the inorganic core comprising the O 2 -evolving center of oxygenic photosynthesis (photosystem II water-oxidation complex, PSII-WOC) are reviewed. These steps, known collectively as photoactivation, involve the photoassembly of the free inorganic cofactors to the cofactor-depleted PSII-(apo-WOC) driven by light and produce the active O 2 -evolving core comprised of Mn 4 CaO x Cl y . We focus on the functional role of the inorganic components as seen through the competition with non-native cofactors ("inorganic mutants") on water oxidation activity, the rate of the photoassembly reaction, and on structural insights gained from EPR spectroscopy of trapped intermediates formed in the initial steps of the assembly reaction. A chemical mechanism for the initial steps in photoactivation is given that is based on these data. Photoactivation experiments offer the powerful insights gained from replacement of the native cofactors, which together with the recent X-ray structural data for the resting holoenzyme provide a deeper understanding of the chemistry of water oxidation. We also review some new directions in research that photoactivation studies have inspired that look at the evolutionary history of this remarkable catalyst.

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“…While CA activity was observed in the manganese-stabilizing protein of the oxygen-evolving complex (PsbO), the recombinant PsbO protein produced in Escherichia coli had no activity without the metal in the active center. When metal ions were added, the highest activity was observed in the presence of manganese ions, while it was much lower in the presence of zinc (Lu et al 2005). It was also found that three proteins from the oxygen-evolving complex possessed CA activity in the presence of manganese ions, but not zinc (Shitov et al 2009).…”

Section: Introductionmentioning

confidence: 97%

Carbonic anhydrase activity in Arabidopsis thaliana thylakoid membrane and fragments enriched with PSI or PSII

et al. 2011

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The procedure of isolating the thylakoids and the thylakoid membrane fragments enriched with either photosystem I or photosystem II (PSI- and PSII-membranes) from Arabidopsis thaliana leaves was developed. It differed from the one used with pea and spinach in durations of detergent treatment and centrifugation, and in concentrations of detergent and Mg(2+) in the media. Both the thylakoid and the fragments preserved carbonic anhydrase (CA) activities. Using nondenaturing electrophoresis followed by detection of CA activity in the gel stained with bromo thymol blue, one low molecular mass carrier of CA activity was found in the PSI-membranes, and two carriers, a low molecular mass one and a high molecular mass one, were found in the PSII-membranes. The proteins in the PSII-membranes differed in their sensitivity to acetazolamide (AA), a specific CA inhibitor. AA at 5 × 10(-7) M inhibited the CA activity of the high molecular mass protein but stimulated the activity of the low molecular mass carrier in the PSII-membranes. At the same concentration, AA moderately inhibited, by 30%, the CA activity of PSI-membranes. CA activity of the PSII-membranes was almost completely suppressed by the lipophilic CA inhibitor, ethoxyzolamide at 10(-9) M, whereas CA activity of the PSI-membranes was inhibited by this inhibitor even at 5 × 10(-7) M just the same as for AA. The observed distribution of CA activity in the thylakoid membranes from A. thaliana was close to the one found in the membranes of pea, evidencing the general pattern of CA activity in the thylakoid membranes of C3-plants.

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Carbonic Anhydrase Activity of the Photosystem II OEC33 Protein from Pea

Cited by 33 publications

References 35 publications

The Basic Properties of the Electronic Structure of the Oxygen-evolving Complex of Photosystem II Are Not Perturbed by Ca2+ Removal

The Basic Properties of the Electronic Structure of the Oxygen-evolving Complex of Photosystem II Are Not Perturbed by Ca2+ Removal

Photoassembly of the water-oxidizing complex in photosystem II

Carbonic anhydrase activity in Arabidopsis thaliana thylakoid membrane and fragments enriched with PSI or PSII

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