scholarly journals Fast enzymatic HCO3- dehydration supports photosynthetic water oxidation in Photosystem II from pea

2021 ◽  
Author(s):  
Alexandr V. Shitov ◽  
Vasily V. Terentyev ◽  
Govindjee Govindjee
Keyword(s):  
Photosystem Ii ◽  
Pisum Sativum ◽  
Water Oxidation ◽  
Photochemical Reactions ◽  
O2 Evolution ◽  
Donor Side ◽  
Psii Photochemistry ◽  
Similar Dependence ◽  
Enzymatic Nature ◽  
Photosynthetic Water Oxidation

Carbonic anhydrase (CA) activity, associated with Photosystem II (PSII) from Pisum sativum, has been shown to enhance water oxidation. But, the nature of the CA activity, its origin and role in photochemistry has been under debate, since the rates of CA reactions, measured earlier, were less than the rates of photochemical reactions. Here, we demonstrate high CA activity in PSII from Pisum sativum, measured by HCO3- dehydration at pH 6.5 (i.e. under optimal condition for PSII photochemistry), with kinetic parameters Km of 2.7 mM; Vmax of 2.74·10-2 mM·sec-1; kcat of 1.16·103 sec-1 and kcat/Km of 4.1·105 M-1 sec-1, showing the enzymatic nature of this activity, which kcat exceeds by ~13 times the rate of PSII, as measured by O2 evolution. The similar dependence of HCO3- dehydration, of the maximal quantum yield of photochemical reactions and of O2 evolution on the ratio of chlorophyll/photochemical reaction center II demonstrate the interconnection of these processes on the electron donor side of PSII. Since the removal of protons is critical for fast water oxidation, and since HCO3- dehydration consumes a proton, we suggest that CA activity, catalyzing very fast removal of protons, supports efficient water oxidation in PSII and, thus, photosynthesis in general.

scholarly journals Electron, proton and hydrogen–atom transfers in photosynthetic water oxidation

2002 ◽  
Vol 357 (1426) ◽  
pp. 1383-1394 ◽  
Author(s):  
Cecilia Tommos
Keyword(s):  
Photosystem Ii ◽  
Proton Transfer ◽  
Water Oxidation ◽  
Oxidation Mechanism ◽  
Bulk Solution ◽  
Hydrogen Atoms ◽  
Redox Active ◽  
Hydrogen Atom Transfers ◽  
Reduce Carbon Dioxide ◽  
Photosynthetic Water Oxidation

When photosynthetic organisms developed so that they could use water as an electron source to reduce carbon dioxide, the stage was set for efficient proliferation. Algae and plants spread globally and provided the foundation for our atmosphere and for O 2 –based chemistry in biological systems. Light–driven water oxidation is catalysed by photosystem II, the active site of which contains a redox–active tyrosine denoted Y Z , a tetramanganese cluster, calcium and chloride. In 1995, Gerald Babcock and co–workers presented the hypothesis that photosynthetic water oxidation occurs as a metallo–radical catalysed process. In this model, the oxidized tyrosine radical is generated by coupled proton/electron transfer and re–reduced by abstracting hydrogen atoms from substrate water or hydroxide–ligated to the manganese cluster. The proposed function of Y Z requires proton transfer from the tyrosine site upon oxidation. The oxidation mechanism of Y Z in an inhibited and O 2 –evolving photosystem II is discussed. Domino–deprotonation from Y Z to the bulk solution is shown to be consistent with a variety of data obtained on metal–depleted samples. Experimental data that suggest that the oxidation of Y Z in O 2 –evolving samples is coupled to proton transfer in a hydrogen–bonding network are described. Finally, a dielectric–dependent model for the proton release that is associated with the catalytic cycle of photosystem II is discussed.

Different sensitivities of photosystem II in green algae and cyanobacteria to phenylurea and phenol-type herbicides: effect on electron donor side

2017 ◽  
Vol 72 (7-8) ◽  
pp. 315-324 ◽  
Author(s):  
Ekaterina K. Yotsova ◽  
Martin A. Stefanov ◽  
Anelia G. Dobrikova ◽  
Emilia L. Apostolova
Keyword(s):  
Photosystem Ii ◽  
Kinetic Parameters ◽  
Oxygen Evolution ◽  
Oxygen Evolving Complex ◽  
Photosynthetic Oxygen Evolution ◽  
Donor Side ◽  
Short Term Treatment ◽  
Psii Photochemistry ◽  
Photosynthetic Oxygen ◽  
Oxygen Evolving

AbstractThe effects of short-term treatment with phenylurea (DCMU, isoproturon) and phenol-type (ioxynil) herbicides on the green algaChlorella kessleriand the cyanobacteriumSynechocystis salinawith different organizations of photosystem II (PSII) were investigated using pulse amplitude modulated (PAM) chlorophyll fluorescence and photosynthetic oxygen evolution measured by polarographic oxygen electrodes (Clark-type and Joliot-type). The photosynthetic oxygen evolution showed stronger inhibition than the PSII photochemistry. The effects of the studied herbicides on both algal and cyanobacterial cells decreased in the following order: DCMU>isoproturon>ioxynil. Furthermore, we observed that the number of blocked PSII centers increased significantly after DCMU treatment (204–250 times) and slightly after ioxynil treatment (19–35 times) in comparison with the control cells. This study suggests that the herbicides affect not only the acceptor side but also the donor side of PSII by modifications of the Mn cluster of the oxygen-evolving complex. We propose that one of the reasons for the different PSII inhibitions caused by herbicides is their influence, in different extents, on the kinetic parameters of the oxygen-evolving reactions (the initial S0−S1state distribution, the number of blocked centers SB, the turnover time of Sistates, misses and double hits). The relationship between the herbicide-induced inhibition and the changes in the kinetic parameters is discussed.

scholarly journals An amino residue that guides the correct photoassembly the water-oxidation complex but not required for high affinity Mn2+ binding

2021 ◽  
Author(s):  
Anton P Avramov ◽  
Minquan Zhang ◽  
Robert L Burnap
Keyword(s):  
Photosystem Ii ◽  
Quantum Efficiency ◽  
Water Oxidation ◽  
Large Fraction ◽  
Wild Type ◽  
Donor Side ◽  
High Affinity ◽  
Initial Binding ◽  
Established Role

The assembly of the Mn4O5Ca cluster of the photosystem II (PSII) starts from the initial binding and photooxidation of the first Mn2+ at a high affinity site (HAS). Recent cryo-EM apo-PSII structures reveal an altered geometry of amino ligands in this region and suggest the involvement of D1-Glu189 ligand in the formation of the HAS. We now find that Gln and Lys substitution mutants photoactivate with reduced quantum efficiency compared to the wild-type. However, the affinity of Mn2+ at the HAS in D1-E189K was very similar to the wild-type (~2.2 μM). Thus, we conclude that D1-E189 does not form the HAS (~2.9 μM) and that the reduced quantum efficiency of photoactivation in D1-E189K cannot be ascribed to the initial photooxidation of Mn2+ at the HAS. Besides reduced quantum efficiency, the D1-E189K mutant exhibits a large fraction of centers that fail to recover activity during photoactivation starting early in the assembly phase, becoming recalcitrant to further assembly. Fluorescence relaxation kinetics indicate on the presence of an alternative route for the charge recombination in Mn-depleted samples in all studied mutants and exclude damage to the photochemical reaction center as the cause for the recalcitrant centers failing to assemble and show that dark incubation of cells reverses some of the inactivation. This reversibility would explain the ability of these mutants to accumulate a significant fraction of active PSII during extended periods of cell growth. The failed recovery in the fraction of inactive centers appears to a reversible mis-assembly involving the accumulation of photooxidized, but non-catalytic high valence Mn at the donor side of photosystem II, and that a reductive mechanism exists for restoration of assembly capacity at sites incurring mis-assembly. Given the established role of Ca2+ in preventing misassembled Mn, we conclude that D1-E189K mutant impairs the ligation of Ca2+ at its effector site in all PSII centers that consequently leads to the mis-assembly resulting in accumulation of non-catalytic Mn at the donor side of PSII. Our data indicate that D1-E189 is not functionally involved in Mn2+ oxidation\binding at the HAS but rather involved in Ca2+ ligation and steps following the initial Mn2+ photooxidation.

scholarly journals Light-driven formation of manganese oxide by today’s photosystem II supports evolutionarily ancient manganese-oxidizing photosynthesis

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Petko Chernev ◽  
Sophie Fischer ◽  
Jutta Hoffmann ◽  
Nicholas Oliver ◽  
Ricardo Assunção ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Manganese Oxide ◽  
Water Oxidation ◽  
Manganese Oxides ◽  
Early Stage ◽  
Oxygenic Photosynthesis ◽  
Oxide Nanoparticles ◽  
Manganese Ions ◽  
Oxide Particles ◽  
Photosynthetic Water Oxidation

AbstractWater oxidation and concomitant dioxygen formation by the manganese-calcium cluster of oxygenic photosynthesis has shaped the biosphere, atmosphere, and geosphere. It has been hypothesized that at an early stage of evolution, before photosynthetic water oxidation became prominent, light-driven formation of manganese oxides from dissolved Mn(2+) ions may have played a key role in bioenergetics and possibly facilitated early geological manganese deposits. Here we report the biochemical evidence for the ability of photosystems to form extended manganese oxide particles. The photochemical redox processes in spinach photosystem-II particles devoid of the manganese-calcium cluster are tracked by visible-light and X-ray spectroscopy. Oxidation of dissolved manganese ions results in high-valent Mn(III,IV)-oxide nanoparticles of the birnessite type bound to photosystem II, with 50-100 manganese ions per photosystem. Having shown that even today’s photosystem II can form birnessite-type oxide particles efficiently, we propose an evolutionary scenario, which involves manganese-oxide production by ancestral photosystems, later followed by down-sizing of protein-bound manganese-oxide nanoparticles to finally yield today’s catalyst of photosynthetic water oxidation.

Inactivation of Photosynthetic O2 Evolution in the Cyanobacterium Anacystis nidulans PCC 6301: Influence of Nitrogen Metabolites and Divalent Cation Concentration

1991 ◽  
Vol 46 (11-12) ◽  
pp. 1024-1032 ◽  
Author(s):  
Gudrun Wälzlein ◽  
Elfriede K. Pistorius
Keyword(s):  
Photosystem Ii ◽  
Nitrogen Source ◽  
Divalent Cation ◽  
Water Oxidation ◽  
Divalent Cations ◽  
Nitrogen Deficiency ◽  
Anacystis Nidulans ◽  
O2 Evolution ◽  
Cation Deficiency

Abstract An investigation about the in vivo inactivation of photosynthetic water oxidation has been carried out in the cyanobacterium Anacystis nidulans (Synechococcus PCC 6301). Photosystem II and photosystem I activity as well as the relative amount of the D1 and manganese stabilizing peptide of photosystem II were determined after growing the cells in nutrient media with variations in the nitrogen source and the concentration of the major divalent cations (Mg2+ and Ca2+). The results show a rapid inactivation of water oxidation in A. nidulans in response to nitrogen deficiency and in response to reduced Mg2+ and Ca2+ concentrations. The inactivation of water oxidation observed under divalent cation deficiency could be greatly accelerated when L-amino acids instead of ammonia or nitrate were used as nitrogen source. Under these conditions inactivation of water oxidation correlated with a rapid loss of D1 and with a slower loss of the manganese stabilizing peptide from photosystem II. A possible regulation of the photosystem II activity in A. nidulans by nitrogen metabolites is suggested.

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