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• W2777333132 abstract "Photoinduced water oxidation at the O2-evolving complex (OEC) of photosystem II (PSII) is a complex process involving a tetramanganese-calcium cluster that is surrounded by a hydrogen-bonded network of water molecules, chloride ions, and amino acid residues. Although the structure of the OEC has remained conserved over eons of evolution, significant differences in the chloride-binding characteristics exist between cyanobacteria and higher plants. An analysis of amino acid residues in and around the OEC has identified residue 87 in the D1 subunit as the only significant difference between PSII in cyanobacteria and higher plants. We substituted the D1-Asn87 residue in the cyanobacterium Synechocystis sp. PCC 6803 (wildtype) with alanine, present in higher plants, or with aspartic acid. We studied PSII core complexes purified from D1-N87A and D1-N87D variant strains to probe the function of the D1-Asn87 residue in the water-oxidation mechanism. EPR spectra of the S2 state and flash-induced FTIR spectra of both D1-N87A and D1-N87D PSII core complexes exhibited characteristics similar to those of wildtype Synechocystis PSII core complexes. However, flash-induced O2-evolution studies revealed a decreased cycling efficiency of the D1-N87D variant, whereas the cycling efficiency of the D1-N87A PSII variant was similar to that of wildtype PSII. Steady-state O2-evolution activity assays revealed that substitution of the D1 residue at position 87 with alanine perturbs the chloride-binding site in the proton-exit channel. These findings provide new insight into the role of the D1-Asn87 site in the water-oxidation mechanism and explain the difference in the chloride-binding properties of cyanobacterial and higher-plant PSII. Photoinduced water oxidation at the O2-evolving complex (OEC) of photosystem II (PSII) is a complex process involving a tetramanganese-calcium cluster that is surrounded by a hydrogen-bonded network of water molecules, chloride ions, and amino acid residues. Although the structure of the OEC has remained conserved over eons of evolution, significant differences in the chloride-binding characteristics exist between cyanobacteria and higher plants. An analysis of amino acid residues in and around the OEC has identified residue 87 in the D1 subunit as the only significant difference between PSII in cyanobacteria and higher plants. We substituted the D1-Asn87 residue in the cyanobacterium Synechocystis sp. PCC 6803 (wildtype) with alanine, present in higher plants, or with aspartic acid. We studied PSII core complexes purified from D1-N87A and D1-N87D variant strains to probe the function of the D1-Asn87 residue in the water-oxidation mechanism. EPR spectra of the S2 state and flash-induced FTIR spectra of both D1-N87A and D1-N87D PSII core complexes exhibited characteristics similar to those of wildtype Synechocystis PSII core complexes. However, flash-induced O2-evolution studies revealed a decreased cycling efficiency of the D1-N87D variant, whereas the cycling efficiency of the D1-N87A PSII variant was similar to that of wildtype PSII. Steady-state O2-evolution activity assays revealed that substitution of the D1 residue at position 87 with alanine perturbs the chloride-binding site in the proton-exit channel. These findings provide new insight into the role of the D1-Asn87 site in the water-oxidation mechanism and explain the difference in the chloride-binding properties of cyanobacterial and higher-plant PSII. Photosystem II (PSII) 4The abbreviations used are: PSIIphotosystem IIChlchlorophyllD1D1 polypeptide of PSIID2D2 polypeptide of PSIIOECoxygen-evolving complex. is a 700-kDa pigment–protein complex responsible for water oxidation in photoautotrophic organisms. The site of water oxidation, known as the oxygen-evolving complex (OEC), consists of a μ-oxo-bridged tetramanganese-calcium cluster ligated by a number of amino acid residues and water molecules (1Suga M. Akita F. Hirata K. Ueno G. Murakami H. Nakajima Y. Shimizu T. Yamashita K. Yamamoto M. Ago H. Shen J.R. Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses.Nature. 2015; 517 (25470056): 99-10310.1038/nature13991Crossref PubMed Scopus (895) Google Scholar). The OEC is surrounded by a network of hydrogen-bonded amino acid residues and water molecules that, along with Cl− ions, play a pivotal role in water oxidation (2Vogt L. Vinyard D.J. Khan S. Brudvig G.W. Oxygen-evolving complex of photosystem II: an analysis of second-shell residues and hydrogen-bonding networks.Curr. Opin. Chem. Biol. 2015; 25 (25621456): 152-15810.1016/j.cbpa.2014.12.040Crossref PubMed Scopus (90) Google Scholar, 3Pokhrel R. Service R.J. Debus R.J. Brudvig G.W. Mutation of lysine 317 in the D2 subunit of photosystem II alters chloride binding and proton transport.Biochemistry. 2013; 52 (23786373): 4758-477310.1021/bi301700uCrossref PubMed Scopus (76) Google Scholar). This process is initiated by photoinduced charge separation via a chlorophyll molecule called P680. The P680·+ species thus formed is reduced by oxidation of the tetramanganese cluster, thereby building up oxidizing equivalents that are used for water oxidation (4McEvoy J.P. Brudvig G.W. Water-splitting chemistry of photosystem II. Chem.Rev. 2006; 106 (17091926): 4455-448310.1021/cr0204294Google Scholar). The process of water oxidation has been shown to proceed via a four-flash cycle called the Kok cycle with the intermediates formed at each step being referred to as Si states (where i = 0–4) (5Kok B. Forbush B. McGloin M. Cooperation of charges in photosynthetic O2 evolution-I: a linear four step mechanism.Photochem. Photobiol. 1970; 11 (5456273): 457-47510.1111/j.1751-1097.1970.tb06017.xCrossref PubMed Scopus (1818) Google Scholar). The transient S4 state has remained elusive so far, whereas the remaining S states have been studied using many experimental methods, especially EPR, FTIR, and extended X-ray absorption fine structure spectroscopy. Information about the S0–S3 states provides valuable insights about water oxidation. photosystem II chlorophyll D1 polypeptide of PSII D2 polypeptide of PSII oxygen-evolving complex. Because of the ease of generation and detection of the S2 state during S-state cycling, this state has been studied extensively. EPR studies of the S2 state in PSII from spinach reveal two distinct spin isomers corresponding to S = 1/2 (g = 2) and S = 5/2 (g = 4.1) states that exist in equilibrium with each other (6Dismukes G.C. Siderer Y. Intermediates of a polynuclear manganese center involved in photosynthetic oxidation of water.Proc. Natl. Acad. Sci. U.S.A. 1981; 78 (16592949): 274-27810.1073/pnas.78.1.274Crossref PubMed Google Scholar, 7Haddy A. Lakshmi K.V. Brudvig G.W. Frank H.A. Q-band EPR of the S2 state of photosystem II confirms an S=5/2 origin of the X-band g=4.1 signal.Biophys. J. 2004; 87 (15454478): 2885-289610.1529/biophysj.104.040238Abstract Full Text Full Text PDF PubMed Scopus (63) Google Scholar8Pokhrel R. Brudvig G.W. Oxygen-evolving complex of photosystem II: correlating structure with spectroscopy.Phys. Chem. Chem. Phys. 2014; 16 (24700294): 11812-1182110.1039/c4cp00493kCrossref PubMed Scopus (62) Google Scholar). In cyanobacterial PSII, however, the S2-state EPR spectrum exhibits only the S = 1/2 spin isomer (8Pokhrel R. Brudvig G.W. Oxygen-evolving complex of photosystem II: correlating structure with spectroscopy.Phys. Chem. Chem. Phys. 2014; 16 (24700294): 11812-1182110.1039/c4cp00493kCrossref PubMed Scopus (62) Google Scholar). This indicates that even though the core of the OEC is highly conserved, there are differences in the surrounding hydrogen-bonding network that affect the equilibrium between these two spin isomers. Because the fundamental process of water oxidation is assumed to remain unchanged over evolution, analyzing the basis and importance of the surrounding amino acid residues is key to understanding the mechanism of water oxidation in greater depth. Previous studies have shown that the equilibrium between the two S2-state isomers can be affected by a number of different factors such as temperature and small molecules like acetate, fluoride, and nitrite (8Pokhrel R. Brudvig G.W. Oxygen-evolving complex of photosystem II: correlating structure with spectroscopy.Phys. Chem. Chem. Phys. 2014; 16 (24700294): 11812-1182110.1039/c4cp00493kCrossref PubMed Scopus (62) Google Scholar, 9Vinyard D.J. Khan S. Askerka M. Batista V.S. Brudvig G.W. Energetics of the S2 state spin isomers of the oxygen-evolving complex of photosystem II.J. Phys. Chem. B. 2017; 121 (28079373): 1020-102510.1021/acs.jpcb.7b00110Crossref PubMed Scopus (35) Google Scholar). All of these factors affect the hydrogen-bonding network surrounding the OEC, thereby stabilizing one of the two isomers. Also, it has been observed that depletion of Cl− favors the S = 5/2 spin isomer in the S2 state of spinach PSII (10Ono T. Zimmermann J.L. Inoue Y. Rutherford A.W. Electron paramagnetic resonance evidence for a modified S-state transition in chloride-depleted photosystem II.Biochim. Biophys. Acta. 1986; 851: 193-20110.1016/0005-2728(86)90125-8Crossref Scopus (144) Google Scholar, 11van Vliet P. Rutherford A.W. Properties of the chloride-depleted oxygen-evolving complex of photosystem II studied by electron paramagnetic resonance.Biochemistry. 1996; 35 (8639664): 1829-183910.1021/bi9514471Crossref PubMed Scopus (78) Google Scholar). This observation, however, has not been seen in cyanobacterial PSII indicating that the Cl−-binding site and its associated hydrogen-bonding network affects the spin isomer distribution differently in the two species (12Boussac A. Ishida N. Sugiura M. Rappaport F. Probing the role of chloride in photosystem II from Thermosynechococcus elongatus by exchanging chloride for iodide.Biochim. Biophys. Acta. 2012; 1817 (22406626): 802-81010.1016/j.bbabio.2012.02.031Crossref PubMed Scopus (32) Google Scholar). Mutations of second-shell residues in cyanobacterial PSII such as D2-K317R, D1-N181A, and D1-N181S have yielded the high-spin, S = 5/2, form of the S2 state, highlighting the importance of these residues in the spin isomer equilibrium distribution (3Pokhrel R. Service R.J. Debus R.J. Brudvig G.W. Mutation of lysine 317 in the D2 subunit of photosystem II alters chloride binding and proton transport.Biochemistry. 2013; 52 (23786373): 4758-477310.1021/bi301700uCrossref PubMed Scopus (76) Google Scholar, 13Pokhrel R. Debus R.J. Brudvig G.W. Probing the effect of mutations of asparagine 181 in the D1 subunit of photosystem II.Biochemistry. 2015; 54 (25680072): 1663-167210.1021/bi501468hCrossref PubMed Scopus (23) Google Scholar). Therefore, it is of interest to focus on changes in the second-shell residues that may impact the hydrogen-bonding network. Sequence alignment studies of the second-shell residues have revealed that the only statistically significant difference between the two species occurs at D1 position 87 (2Vogt L. Vinyard D.J. Khan S. Brudvig G.W. Oxygen-evolving complex of photosystem II: an analysis of second-shell residues and hydrogen-bonding networks.Curr. Opin. Chem. Biol. 2015; 25 (25621456): 152-15810.1016/j.cbpa.2014.12.040Crossref PubMed Scopus (90) Google Scholar). This site is occupied by an asparagine residue in a significant majority of cyanobacterial PSII including Synechocystis PCC 6803 as opposed to an alanine residue in spinach PSII. Furthermore, this residue is an important part of the “narrow” channel of hydrogen-bonded waters whose role is yet to be determined (2Vogt L. Vinyard D.J. Khan S. Brudvig G.W. Oxygen-evolving complex of photosystem II: an analysis of second-shell residues and hydrogen-bonding networks.Curr. Opin. Chem. Biol. 2015; 25 (25621456): 152-15810.1016/j.cbpa.2014.12.040Crossref PubMed Scopus (90) Google Scholar). The hydrogen-bonding network surrounding the manganese cluster is extensive; therefore, perturbation at any point might be propagated over a long distance and can affect remote sites like the Cl−-binding site which is ˜13 Å from D1 residue 87. Fig. 1 shows the extensive hydrogen-bonding network connected to D1 residue 87 in cyanobacterial PSII obtained from Thermosynechococcus elongatus (Protein Data Bank code 3WU2). Based on these observations it is therefore hypothesized that substitution of D1 residue 87 in cyanobacterial PSII would be able to effect some of the changes that are different in the two species. The current study deals with characterization of substitutions of D1 residue 87, specifically D1-N87A and D1-N87D. In addition to understanding the role of this site, our study also has uncovered some of the fundamental aspects that are different between the two species and hence provides new insight into the mechanism of water oxidation. To investigate the significance of the difference in D1 residue 87 between spinach PSII and cyanobacterial PSII, the D1-N87A and D1-N87D mutations were constructed in Synechocystis sp. PCC 6803. D1-N87A cells and D1-N87D cells exhibit photoautotrophic growth. The doubling times of D1-N87A and D1-N87D cells were 26 and 21 h, respectively, compared with 14 h for wildtype cells (Fig. S1). The light-saturated O2-evolution rates of D1-N87A and D1-N87D cells were 64 ± 4 and 36 ± 2% compared with the rate of wildtype cells, respectively (Table S1 and Note S1). On the basis of the maximum fluorescence yields (Fmax − F0) of wildtype, D1-N87A, and D1-N87D cells, the PSII contents of D1-N87A and D1-N87D cells were estimated to be 73 ± 5 and 36 ± 4% compared with wildtype cells, respectively (Fig. S2, Table S1, and Note S1). On the basis of measurements of the kinetics of charge recombination between QA− and the donor side of PSII following 5 s of actinic illumination in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), it was estimated that 10–14% of PSII reaction centers in D1-N87A and D1-N87D cells lack Mn4CaO5 clusters in vivo (Fig. S3 and Note S2). The presence of PSII reaction centers lacking Mn4CaO5 clusters implies that the Mn4CaO5 cluster is assembled less efficiently or is less stable in D1-N87A and D1-N87D cells compared with wildtype. The light-saturated rates of O2 evolution in PSII core complexes isolated from D1-N87D and D1-N87A cells were 886 ± 28 and 3100 ± 56 μmol of O2 (mg of Chl)−1 h−1, respectively, compared with 3400 ± 83 μmol of O2 (mg of Chl)−1 h−1 for wildtype PSII core complexes under similar assay conditions using a buffer containing 60 mm Cl− (Table 1). The lower PSII activity in the D1-N87D core complex can be due to inefficient assembly of the OEC, impaired S-state cycling or due to inactivation during biochemical isolation of PSII core complexes.Table 1Effect of Cl− on O2-evolution activitySamplePSII activity+ 60 mm Cl−+ 0.1 mm Cl−μmol of O2 (mg of chl)−1 h−1Synechocystis (wildtype) PSII core complexes3400 ± 832992 ± 35D1-N87A PSII core complexes3100 ± 561360 ± 46D1-N87D PSII core complexes886 ± 28744 ± 15Spinach PSII membranes650 ± 35286 ± 29 Open table in a new tab To study the effect of Cl− on the steady-state oxygen evolution of D1-N87A and D1-N87D PSII, the PSII core complexes were suspended in a buffer containing 0.1 mm Cl−. The light-saturated activity of D1-N87D and D1-N87A PSII under this condition is given in Table 1. Under low Cl− conditions, the oxygen-evolution activity of D1-N87D PSII decreased by 16% relative to Cl−-sufficient conditions. The Cl− dependence of D1-N87D PSII is comparable with that of wildtype Synechocystis PSII core complexes, which exhibit a decrease in activity of only 12% under similar experimental conditions. However, the Cl− dependence of D1-N87A PSII is markedly different from wildtype Synechocystis PSII, with a 56% decrease in the oxygen-evolution activity in low Cl− conditions relative to Cl−-sufficient conditions; notably, this decrease is comparable with the 52% decrease observed for spinach PSII membranes (Table 1). These results demonstrate that the D1-N87A mutation modulates the Cl−-binding site, causing the Cl− dependence of PSII activity to be similar to spinach PSII. It is interesting, however, that the D1-N87D substitution has little effect on Cl− binding. Based on these results, we investigated the effect of these single-point mutations at D1 residue 87 on the binding affinity of chloride. The Cl− concentrations were varied from 0.1 to 5 mm, and their effect on PSII activity was measured. The observation of biphasic binding curves (Fig. 2) suggests the presence of at least two types of Cl−-binding sites: one in which the bound chloride is exchangeable with free chloride (which titrates with a binding constant of KD) and another non-exchangeable site (which gives activity in the absence of added chloride). The binding curves were computed by fitting the data to a biphasic Michaelis–Menten equation (Equation 1), Vobs=f×Vmax+(1−f)×Vmax×[Cl−]KD+[Cl−](1) where Vobs is the observed rate of oxygen evolution, Vmax is the maximum observed activity which is normalized to 1, f is the fraction of centers with non-exchangeable Cl−, and KD is the binding constant of the exchangeable Cl−. The measured KD values for Cl− in D1-N87A and D1-N87D PSII are 0.730 ± 0.218 mm (f = 0.4) and 1.35 ± 0.956 mm (f = 0.8), respectively, which fall within the range of KD values obtained for Cl− in spinach PSII (0.5–0.7 mm) (14Lindberg K. Andréasson L.-E. A one-site, two-state model for the binding of anions in photosystem II.Biochemistry. 1996; 35 (8916911): 14259-1426710.1021/bi961244sCrossref PubMed Scopus (89) Google Scholar, 15Kühne H. Szalai V.A. Brudvig G.W. Competitive binding of acetate and chloride in photosystem II.Biochemistry. 1999; 38 (10350479): 6604-661310.1021/bi990341tCrossref PubMed Scopus (56) Google Scholar16Cooper I.B. Barry B.A. Azide as a probe of proton transfer reactions in photosynthetic oxygen evolution.Biophys. J. 2008; 95 (18805932): 5843-585010.1529/biophysj.108.136879Abstract Full Text Full Text PDF PubMed Scopus (9) Google Scholar). These results indicate that the binding environment of the exchangeable Cl− in the two D1-Asn87–substituted PSII samples is similar to that in spinach PSII. However, the fraction of exchangeable Cl− is much larger in D1-N87A Synechocystis PSII and spinach PSII than in wildtype Synechocystis PSII and D1-N87D Synechocystis PSII. EPR experiments recording the S1- and S2-state spectra of spinach PSII membranes, and Synechocystis wildtype, D1-N87A and D1-N87D PSII core complexes were performed (S2-minus-S1 difference spectra shown in Fig. 3, unsubtracted spectra are included in Fig. S4, EPR spectra of spinach PSII membranes are included in Fig. S9). EPR spectra of D1-N87A were also collected after changing the cryoprotectant to sucrose. The spectrum in the presence of sucrose is similar to the spectrum in 10% (v/v) glycerol as cyoprotectant (Fig. S10). The dark spectra corresponding to the S1 state exhibit a cytochrome c550 signal. Upon 200 K illumination, the OEC advances to the S2 state, which is characterized by the presence of a g = 2 multiline EPR signal. The multiline signal was observed in wildtype, D1-N87A, and D1-N87D PSII (Fig. 3). However, the S = 5/2 spin isomer giving the S2-state g = 4.1 signal that is observed under these conditions in spinach PSII membranes was absent in both D1-N87D and D1-N87A PSII. In addition, the S2-minus-S1 difference spectra show a light-induced cytochrome b559 signal at g = 3. The fraction of PSII centers lacking a functional OEC gives rise to this signal when the sample is illuminated at 200 K. The intensities of g = 2 multiline signal of D1-N87D and D1-N87A PSII are smaller relative to wildtype PSII for a similar chlorophyll concentration. Both the weaker g = 2 multiline signal and the 200 K light-induced cytochrome b559 signal indicate that the D1-N87D and D1-N87A PSII samples have fewer functional OECs, consistent with the lower oxygen-evolution activity observed for the EPR samples. The mid-frequency FTIR difference spectra induced by four successive flashes given to wildtype and D1-N87D PSII core complexes are compared in Fig. 4 (black and red traces, respectively). The spectra that are induced by the first, second, third, and fourth flashes correspond predominantly to the S2-minus-S1, S3-minus-S2, S0-minus-S3, and S1-minus-S0 FTIR difference spectra, respectively (17Noguchi T. Monitoring the reactions of photosynthetic water oxidation using infrared spectroscopy.Biomed. Spectrosc. Imaging. 2013; 2: 115-12810.3233/BSI-130040Crossref Scopus (25) Google Scholar18Chu H.-A. Fourier transform infrared difference spectroscopy for studying the molecular mechanism of photosynthetic water oxidation.Front. Plant Sci. 2013; 4 (23734156): 146Crossref PubMed Scopus (36) Google Scholar, 19Noguchi T. Fourier transform infrared analysis of the photosynthetic oxygen-evolving center.Coord. Chem. Rev. 2008; 252: 336-34610.1016/j.ccr.2007.05.001Crossref Scopus (93) Google Scholar20Noguchi T. Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution.Photosynth. Res. 2007; 91 (17279438): 59-6910.1007/s11120-007-9137-5Crossref PubMed Scopus (72) Google Scholar). The mid-frequency S2-minus-S1 spectrum of D1-N87D PSII core complexes showed substantial changes compared with wildtype PSII throughout the mid-frequency region (upper red trace in Fig. 4). In the carbonyl stretching [ν(C=O)] region, the negative feature at 1746 cm−1 was broadened slightly and shifted ˜2 cm−1 to higher frequency. In the amide I region, the negative features at 1689 and 1680 cm−1 were replaced by positive features at 1684 and 1670 cm−1, and the negative feature at 1629 cm−1 was replaced by a negative feature at 1641 cm−1. These features correspond to amide I modes because they shift significantly to lower frequencies after global incorporation of 13C (21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar, 22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar) but not appreciably after global incorporation of 15N (21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar, 22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar). In the overlapping asymmetric carboxylate stretching [νasym(COO−)]/amide II region, the positive feature at 1586 cm−1 was shifted ˜3 cm−1 to higher frequency and diminished in amplitude, the 1560(−), 1551(+), and 1544(−) cm−1 features shifted downward, and the 1523(−) cm−1 feature was diminished. The 1587 cm−1 feature corresponds to a νasym(COO−) mode because it shifts 30–35 cm−1 to lower frequency after global incorporation of 13C (21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar, 23Noguchi T. Sugiura M. Analysis of flash-induced FTIR difference spectra of the S-state cycle in the photosynthetic water-oxidizing complex by uniform 15N and 13C isotope labeling.Biochemistry. 2003; 42 (12755605): 6035-604210.1021/bi0341612Crossref PubMed Scopus (119) Google Scholar24Noguchi T. Sugiura M. Inoue Y. Itoh K. Tasumi M. FTIR studies on the amino-acid ligands of the photosynthetic oxygen-evolving Mn-cluster.in: Fourier Transform Spectroscopy: Twelfth International Conference. Waseda University Press, Tokyo, Japan1999: 459-460Google Scholar) but is largely insensitive to the global incorporation of 15N (3Pokhrel R. Service R.J. Debus R.J. Brudvig G.W. Mutation of lysine 317 in the D2 subunit of photosystem II alters chloride binding and proton transport.Biochemistry. 2013; 52 (23786373): 4758-477310.1021/bi301700uCrossref PubMed Scopus (76) Google Scholar, 21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar, 22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar23Noguchi T. Sugiura M. Analysis of flash-induced FTIR difference spectra of the S-state cycle in the photosynthetic water-oxidizing complex by uniform 15N and 13C isotope labeling.Biochemistry. 2003; 42 (12755605): 6035-604210.1021/bi0341612Crossref PubMed Scopus (119) Google Scholar, 25Service R.J. Yano J. McConnell I. Hwang H.J. Niks D. Hille R. Wydrzynski T. Burnap R.L. Hillier W. Debus R.J. Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem II.Biochemistry. 2011; 50 (21114287): 63-8110.1021/bi1015937Crossref PubMed Scopus (50) Google Scholar). The 1560(−), 1551(+), and 1544(−) features correspond to amide II modes because they shift appreciably to lower frequencies after global incorporation of either 13C (21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar, 23Noguchi T. Sugiura M. Analysis of flash-induced FTIR difference spectra of the S-state cycle in the photosynthetic water-oxidizing complex by uniform 15N and 13C isotope labeling.Biochemistry. 2003; 42 (12755605): 6035-604210.1021/bi0341612Crossref PubMed Scopus (119) Google Scholar24Noguchi T. Sugiura M. Inoue Y. Itoh K. Tasumi M. FTIR studies on the amino-acid ligands of the photosynthetic oxygen-evolving Mn-cluster.in: Fourier Transform Spectroscopy: Twelfth International Conference. Waseda University Press, Tokyo, Japan1999: 459-460Google Scholar) or 15N (3Pokhrel R. Service R.J. Debus R.J. Brudvig G.W. Mutation of lysine 317 in the D2 subunit of photosystem II alters chloride binding and proton transport.Biochemistry. 2013; 52 (23786373): 4758-477310.1021/bi301700uCrossref PubMed Scopus (76) Google Scholar, 21Yamanari T. Kimura Y. Mizusawa N. Ishii A. Ono T-a. Mid-to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.Biochemistry. 2004; 43 (15182190): 7479-749010.1021/bi0362323Crossref PubMed Scopus (51) Google Scholar, 22Kimura Y. Mizusawa N. Ishii A. Yamanari T. Ono T.-A. Changes of low-frequency vibrational modes induced by universal 15N- and 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex.Biochemistry. 2003; 42 (14609327): 13170-1317710.1021/bi035420qCrossref PubMed Scopus (68) Google Scholar23Noguchi T. Sugiura M. Analysis of flash-induced FTIR difference spectra of the S-state cycle in the photosynthetic water-oxidizing complex by uniform 15N and 13C isotope labeling.Biochemistry. 2003; 42 (12755605): 6035-604210.1021/bi0341612Crossref PubMed Scopus (119) Google Scholar, 25Service R.J. Yano J. McConnell I. Hwang H.J. Niks D. Hille R. Wydrzynski T. Burnap R.L. Hillier W. Debus R.J. Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem II.Biochemistry. 2011; 50 (21114287): 63-8110.1021/bi1015937Crossref PubMed Scopus (50) Google Scholar). In the symmetric carboxylate stretching [νsym(COO−)] region, the positive shoulder at 1432 cm−1 was eliminated; features at 1415(−), 1410(+), and 1400(−) cm−1 were shifted ˜2 cm−1 to higher frequencies; features at 1354(−) and 1343(+) cm−1 were shifted 4–5 cm−1 to lower frequencies; and a negative feature at 1384 cm−1 appeared. The mid-frequency S2-minus-S1 spectrum of D1-N87A PSII core complexes (Fig. S6, upper red trace) showed changes similar to those observed for D1-N87D PSII core complexes. The mid-frequency S3-minus-S2, S0-minus-S3, and S1-minus-S0 difference spectra of D1-N87D PSII core complexes (Fig. 4, middle three pairs of spectra) showed" @default.
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• W2777333132 title "Substitution of the D1-Asn87 site in photosystem II of cyanobacteria mimics the chloride-binding characteristics of spinach photosystem II" @default.
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