A photosystem II-associated carbonic anhydrase regulates the efficiency of photosynthetic oxygen evolution

Villarejo, Arsenio; Shutova, Tatiana; Moskvin, Oleg V.; Forssén, Magnus; Klimov, Vyacheslav V.; Samuelsson, Göran

doi:10.1093/emboj/21.8.1930

Cited by 96 publications

(98 citation statements)

References 33 publications

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“…This would have a physiological meaning, ensuring the prompt removal of protons released during water oxidation. The latter process can be a part of the system preventing photoinhibition, as was proposed previously [8].…”

Section: Discussionmentioning

confidence: 59%

“…Previously, we revealed that the pea thylakoid membrane fragments enriched with PSII demonstrated a noticeable dehydrase CA activity only after the treatments either with detergent or salt, while this activity was high in the core complex of PSII [6,7]. The presence of CA activity was also found in PSII core complexes from Chlamydomonas reinhardtii [8]. Using the affinity electrophoresis and affinity chromatography of n-dodecyl-b-maltoside (DM) extract of PSII membrane isolated from wheat, we got in the present work new convincing data, which permitted to locate PSII CA activity in the core complex.…”

Section: Introductionmentioning

confidence: 88%

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Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

et al. 2004

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The thylakoid membrane containing photosystem II (PSII membranes) from pea and wheat leaves catalyzed the reaction of CO 2 hydration with low rate, which increased after their incubation either with Triton X-100, up to Triton/chlorophyll ratio 1:1, or 1 M CaCl 2 . The presence of the inhibitor of CAs, p-aminomethylbenzensulfonamide (mafenide), at the start line in the course of electrophoresis of PSII membranes solubilized by n-dodecyl-b-maltoside (DM) decreased the amount of PSII core complex in the gel. The elution of PSII core complex from the column with immobilized mafenide occurred only either by mafenide or another inhibitor of CAs, ethoxyzolamide. The above results led to a conclusion that membrane-bound CA activity associated with PSII is situated in the core complex.

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Section: Discussionmentioning

confidence: 59%

Section: Introductionmentioning

confidence: 88%

Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

et al. 2004

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“…As Cah-3 is known to be associated with polypeptides of photosystem (PS) II of C. reinhardtii thylakoid membranes (Park et al, 1999;Villarejo et al, 2002), it was necessary to be sure that the signal observed in the cell envelope fraction of M. chthonoplastes did not result from cross-contamination of this fraction with thylakoid membranes from the cyanobacterium. Antibodies against D1 (PsbA), a major protein of PS II, was used as a specific marker for thylakoid membranes (Nishiyama et al, 2001).…”

Section: Identification Of M Chthonoplastes Extracellular A-camentioning

confidence: 99%

Extracellular carbonic anhydrases of the stromatolite-forming cyanobacterium Microcoleus chthonoplastes

et al. 2007

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“…In the present study using higher plant PSII membranes, we specifically evaluate a recently suggested role of weakly bound HCO − 3 , namely, that it acts as an acceptor for, and transporter of, protons produced by water splitting in the OEC (20)(21)(22).…”

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confidence: 99%

Mobile hydrogen carbonate acts as proton acceptor in photosynthetic water oxidation

Koroidov

Shevela

Shutova

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Cyanobacteria, algae, and plants oxidize water to the O 2 we breathe, and consume CO 2 during the synthesis of biomass. Although these vital processes are functionally and structurally well separated in photosynthetic organisms, there is a long-debated role for CO 2 /HCO − 3 in water oxidation. Using membrane-inlet mass spectrometry we demonstrate that HCO − 3 acts as a mobile proton acceptor that helps to transport the protons produced inside of photosystem II by water oxidation out into the chloroplast's lumen, resulting in a light-driven production of O 2 and CO 2 . Depletion of HCO − 3 from the media leads, in the absence of added buffers, to a reversible down-regulation of O 2 production by about 20%. These findings add a previously unidentified component to the regulatory network of oxygenic photosynthesis and conclude the more than 50-y-long quest for the function of CO 2 / HCO − 3 in photosynthetic water oxidation.O xygenic photosynthesis in cyanobacteria, algae, and higher plants leads to the reduction of atmospheric CO 2 to energy-rich carbohydrates. The electrons needed for this process are extracted in a cyclic, light-driven process from water that is split into dioxygen (O 2 ) and protons. This reaction is catalyzed by a penta-μ-oxo bridged tetra-manganese calcium cluster (Mn 4 CaO 5 ) within the oxygen-evolving complex (OEC) of photosystem II (PSII) (1-4). The possible roles of inorganic carbon, C i ðC i = CO 2 ; H 2 CO 3 ; HCO − 3 ; CO 2− 3 Þ, in this process have been a controversial issue ever since Otto Warburg and Günter Krippahl (5) reported in 1958 that oxygen evolution by PSII strictly depends on CO 2 and therefore has to be based on the photolysis of H 2 CO 3 ("Kohlensäure") and not of water. These first experiments were indirect and, as became apparent later, were wrongly interpreted (6-8). Several research groups followed up on these initial results and identified two possible sites of C i interaction within PSII (reviewed in refs. 9-12). Functional and spectroscopic studies showed that HCO − 3 facilitates the reduction of the secondary plastoquinone electron acceptor (Q B ) of PSII by participating in the protonation of Q 2− B . Binding of HCO − 3 (or CO 2− 3 ) to the nonheme Fe between the quinones Q A and Q B was recently confirmed by X-ray crystallography (3,13,14). Despite this functional role at the acceptor side, the very tight binding of HCO − 3 to this site makes it impossible for the activity of PSII to be affected by changing the C i level of the medium; instead inhibitors such as formate need to be added to induce the acceptor-side effect (15). Consequently, the watersplitting electron-donor side of PSII has also been studied intensively (for recent reviews, see refs. 11 and 12). Although a tight binding of C i near the Mn 4 CaO 5 cluster is excluded on the basis of X-ray crystallography (3, 14), FTIR spectroscopy (16), and mass spectrometry (17, 18), the possibility that a weakly bound HCO − 3 affects the activity of PSII at the donor side remains a viable option (reviewed i...

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A photosystem II-associated carbonic anhydrase regulates the efficiency of photosynthetic oxygen evolution

Cited by 96 publications

References 33 publications

Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

Extracellular carbonic anhydrases of the stromatolite-forming cyanobacterium Microcoleus chthonoplastes

Mobile hydrogen carbonate acts as proton acceptor in photosynthetic water oxidation

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