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

Khristin, M. S.; Ignatova, L. K.; Rudenko, Natalia N.; Иванов, Б. Н.; Klimov, Vyacheslav V.

doi:10.1016/j.febslet.2004.10.001

Cited by 29 publications

(14 citation statements)

References 18 publications

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“…Lu and Stemler (2002) and Moskvin et al (2004) found high CA activity of the core complex of the PSII from maize and pea, respectively. Khristin et al (2004) showed that a high molecular mass carrier of CA activity in the PSII-membranes appeared as a part of the core complex of the PSII, and discussed the possibility that such an activity could be the property of a specific structure, and not of an individual protein. This proposition may be compared to the presence of only one peak upon Triton treatment of PSII-membranes (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…Later, Lu and Stemler (2002) stated that two sources of CA activity could be associated with PSII in maize mesophyll chloroplasts. Khristin et al (2004) found that at least a part of the CA activity of thylakoid membrane fragments enriched with PSII (PSII-membranes) from wheat was connected with the core complex of this photosystem. Ignatova et al (2006) presented evidence of the presence of two types of CA activity in the PSIImembranes isolated from pea leaves, and found that one of the CA activities was associated with a low molecular mass protein.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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

et al. 2011

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“…Strictly speaking, however, these data are still compatible with a catalytic role of bicarbonate if the equilibrium between water, CO 2 , and bicarbonate is rapidly installed, as mediated, for example, by a carbonic anhydrase (CA; Silverman and Tu, 1975;Tu and Silverman, 1975). An intrinsic CA activity is indeed linked to the core and/or extrinsic proteins of PSII (Dai et al, 2001;Stemler, 2002;Villarejo et al, 2002;Khristin et al, 2004). The above-cited mass-spectrometric experiments were not designed to specifically address the bicarbonate question, and therefore the CA activity was not assessed in detail.…”

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confidence: 99%

Evidence That Bicarbonate Is Not the Substrate in Photosynthetic Oxygen Evolution

et al. 2005

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(J.C., W.J.); and Max-PlanckInstitut fü r Bioanorganische Chemie, 45470 Muelheim an der Ruhr, Germany (K.B., J.M.)It is widely accepted that the oxygen produced by photosystem II of cyanobacteria, algae, and plants is derived from water. Earlier proposals that bicarbonate may serve as substrate or catalytic intermediate are almost forgotten, though not rigorously disproved. These latter proposals imply that CO 2 is an intermediate product of oxygen production in addition to O 2 . In this work, we investigated this possible role of exchangeable HCO 3 2 in oxygen evolution in two independent ways. (1) We studied a possible product inhibition of the electron transfer into the catalytic Mn 4 Ca complex during the oxygen-evolving reaction by greatly increasing the pressure of CO 2 . This was monitored by absorption transients in the near UV. We found that a 3,000-fold increase of the CO 2 pressure over ambient conditions did not affect the UV transient, whereas the S 3 / S 4 / S 0 transition was half-inhibited by raising the O 2 pressure only 10-fold over ambient, as previously established. (2) The flash-induced O 2 and CO 2 production by photosystem II was followed simultaneously with membrane inlet mass spectrometry under approximately 15% H 2 18 O enrichment. Light flashes that revealed the known oscillatory O 2 release failed to produce any oscillatory CO 2 signal. Both types of results exclude that exchangeable bicarbonate is the substrate for (and CO 2 an intermediate product of) oxygen evolution by photosynthesis. The possibility that a tightly bound carbonate or bicarbonate is a cofactor of photosynthetic water oxidation has remained.

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“…The evidence in favour of the presence of two sources of CA activity in PSII-membranes was also obtained for pea [58,64] and for arabidopsis [62]. The CA activity appeared in solution after treating PSII-membranes either with salts in high concentration [58,70] or with detergents [64], but a significant part of the CA activity remained in PSII membranes [58,64,70,71,72]. The presence of two sources of CA activity in PSII was also revealed after native electrophoresis of detergent-treated PSII membranes from pea and arabidopsis: CA activity was detected in the gel band containing the low molecular mass proteins as well as in the upper gel area containing proteins associated with the PSII core complex [62,64,73].…”

Section: Carbonic Anhydrases In Chloroplastsmentioning

confidence: 93%

Carbonic Anhydrases in Photosynthesizing Cells of C3 Higher Plants

et al. 2019

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The review presents data on the location, nature, properties, number, and expression of carbonic anhydrase genes in the photosynthesizing cells of C3 plants. The available data about the presence of carbonic anhydrases in plasma membrane, cytoplasm, mitochondria, chloroplast stroma and thylakoids are scrutinized. Special attention was paid to the presence of carbonic anhydrase activities in the different parts of thylakoids, and on collation of sources of these activities with enzymes encoded by the established genes of carbonic anhydrases. The data are presented to show that the consistent incorporation of carbonic anhydrases belonging to different families of these enzymes forms a coherent system of CO2 molecules transport from air to chloroplasts in photosynthesizing cells, where they are included in organic molecules in the carboxylation reaction. It is discussed that the manifestation of the activity of a certain carbonic anhydrase depends on environmental conditions and the stage of ontogenesis.

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

Cited by 29 publications

References 18 publications

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

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

Evidence That Bicarbonate Is Not the Substrate in Photosynthetic Oxygen Evolution

Carbonic Anhydrases in Photosynthesizing Cells of C3 Higher Plants

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