PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21988105-0 2011 Neutron structure of human carbonic anhydrase II: a hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0. Water 68-73 carbonic anhydrase 2 Homo sapiens 27-48 21754317-1 2011 In title compound, [Ca(C(7)H(5)O(2))(2)(C(7)H(6)O(2))(H(2)O)](n), the eightfold-coordinated Ca(II) ion is bonded to four carboxyl-ate O atoms from two benzoate ions, an O atom from benzoic acid and a water O atom. Water 54-60 carbonic anhydrase 2 Homo sapiens 92-98 22090875-2 2011 The Ca(II) atom is octa-coordinated by two O atoms from two water mol-ecules and six O atoms from four acetate ligands. Water 60-65 carbonic anhydrase 2 Homo sapiens 4-10 21612240-1 2011 The binding of Sr(II), Ca(II), Mg(II), Ba(II), Mn(II), Zn(II), and Cd(II) to silica/water interfaces functionalized with A(15)T(6) oligonucleotides was quantified at pH 7 and 10 mM NaCl using the Eisenthal chi((3)) technique. Water 84-89 carbonic anhydrase 2 Homo sapiens 23-29 21754317-1 2011 In title compound, [Ca(C(7)H(5)O(2))(2)(C(7)H(6)O(2))(H(2)O)](n), the eightfold-coordinated Ca(II) ion is bonded to four carboxyl-ate O atoms from two benzoate ions, an O atom from benzoic acid and a water O atom. Water 200-205 carbonic anhydrase 2 Homo sapiens 92-98 21522881-1 2011 In the polymeric title compound, [Ca(C(7)H(3)NO(4))(H(2)O)(C(2)H(6)OS)](n), the Ca(II) ion is coordinated in a distorted penta-gonal-bipyramidal CdNO(6) geometry. Water 52-57 carbonic anhydrase 2 Homo sapiens 80-86 21332115-5 2011 Structural characterization of the library compounds in complex with human CA II revealed a novel binding mode whereby a methyl ester interacts via a water molecule with the active site zinc. Water 150-155 carbonic anhydrase 2 Homo sapiens 75-80 21588864-1 2010 In the title complex, [Ca(C(10)H(6)NO(2))(2)(H(2)O)(2)](n), the Ca(II) ion is eight-coordinated by six carboxyl-ate O atoms from four separate quinoline-3-carboxyl-ate ligands, two of which are bidentate chelate and two bridging, and two water mol-ecules in a distorted square-anti-prismatic geometry. Water 45-50 carbonic anhydrase 2 Homo sapiens 64-70 21588864-1 2010 In the title complex, [Ca(C(10)H(6)NO(2))(2)(H(2)O)(2)](n), the Ca(II) ion is eight-coordinated by six carboxyl-ate O atoms from four separate quinoline-3-carboxyl-ate ligands, two of which are bidentate chelate and two bridging, and two water mol-ecules in a distorted square-anti-prismatic geometry. Water 238-243 carbonic anhydrase 2 Homo sapiens 64-70 20598552-4 2010 An X-ray crystal structure of hCA II in complex with 4-(7-methoxy-coumarin-4-yl-acetamido)-benzenesulfonamide (KI of 9.1 nM against hCA II) showed the intact inhibitor coordinated to the zinc ion from the enzyme active site by the sulfonamide moiety, and participating in a edge-to-face stacking with Phe131, in addition to other hydrophobic and hydrophilic interactions with water molecules and amino acid residues from the active site. Water 376-381 carbonic anhydrase 2 Homo sapiens 30-36 20578724-1 2010 The catalysis of CO(2) hydration by human carbonic anhydrase II (HCA II) is limited in maximal velocity by proton transfer from a zinc-bound water molecule to the proton shuttle His64. Water 141-146 carbonic anhydrase 2 Homo sapiens 42-63 20598552-4 2010 An X-ray crystal structure of hCA II in complex with 4-(7-methoxy-coumarin-4-yl-acetamido)-benzenesulfonamide (KI of 9.1 nM against hCA II) showed the intact inhibitor coordinated to the zinc ion from the enzyme active site by the sulfonamide moiety, and participating in a edge-to-face stacking with Phe131, in addition to other hydrophobic and hydrophilic interactions with water molecules and amino acid residues from the active site. Water 376-381 carbonic anhydrase 2 Homo sapiens 132-138 20000378-1 2010 The crystal structure of human carbonic anhydrase II (HCA II) obtained at 0.9 A resolution reveals that a water molecule, termed deep water, Dw, and bound in a hydrophobic pocket of the active site forms a short, strong hydrogen bond with the zinc-bound solvent molecule, a conclusion based on the observed oxygen-oxygen distance of 2.45 A. Water 106-111 carbonic anhydrase 2 Homo sapiens 31-52 20000378-1 2010 The crystal structure of human carbonic anhydrase II (HCA II) obtained at 0.9 A resolution reveals that a water molecule, termed deep water, Dw, and bound in a hydrophobic pocket of the active site forms a short, strong hydrogen bond with the zinc-bound solvent molecule, a conclusion based on the observed oxygen-oxygen distance of 2.45 A. Water 134-139 carbonic anhydrase 2 Homo sapiens 31-52 20410571-7 2010 Good validation was obtained on applications of the two phases for the separation and determination of Ca(II) in natural water and pharmaceutical samples with no matrix interferences at pH 10.00 under dynamic conditions prior to determination by AAS. Water 121-126 carbonic anhydrase 2 Homo sapiens 103-109 19407386-3 2009 A joint X-ray and neutron crystallographic study has been initiated to determine the specific water network and the protonation states of the hydrophilic residues that coordinate it in human carbonic anhydrase II. Water 94-99 carbonic anhydrase 2 Homo sapiens 191-212 18441928-3 2008 The efficiency of calcite barrier to control phosphorus release from sediments will increase with the increment of Ca2+ concentration of overlying water and barrier thickness. Water 147-152 carbonic anhydrase 2 Homo sapiens 115-118 19119014-5 2009 Examining the four X-ray crystal structures of their CA II adducts, we observed several (2-3) active site water molecules interacting with the chlorthalidone, trichloromethiazide, and furosemide scaffolds which may be responsible for this important difference of activity. Water 106-111 carbonic anhydrase 2 Homo sapiens 53-58 19119014-7 2009 Chlorthalidone bound within the CA II active site is in an enolic (lactimic) tautomeric form, with the enolic OH also participating in two strong hydrogen bonds with Asn67 and a water molecule. Water 178-183 carbonic anhydrase 2 Homo sapiens 32-37 19115843-5 2009 In the X-ray crystal structures of the CA II-chlorthalidone adduct three active site water molecules interacting with the inhibitor scaffold were observed that lack in the corresponding indapamide adduct. Water 85-90 carbonic anhydrase 2 Homo sapiens 39-44 19030623-5 2008 Observed first-order rate constants in the presence of 1-2 mM Mg(II) or Ca(II) in neutral and weakly basic solutions were 10(8)-10(11) times higher than those for background hydrolysis at the same pH while in water additions of up to 50 mM metal produced <100-fold accelerations. Water 209-214 carbonic anhydrase 2 Homo sapiens 72-78 21202200-1 2008 In the title coordination polymer, {[Ca(C(8)H(5)Cl(2)O(3))(2)(H(2)O)(2)] H(2)O}(n), the Ca(II) atom is eight-coordinated by six O atoms from four different (2,4-dichloro-phen-oxy)acetate ligands and two water mol-ecules, and displays a distorted square-anti-prismatic coordination geometry. Water 62-67 carbonic anhydrase 2 Homo sapiens 88-94 21202200-1 2008 In the title coordination polymer, {[Ca(C(8)H(5)Cl(2)O(3))(2)(H(2)O)(2)] H(2)O}(n), the Ca(II) atom is eight-coordinated by six O atoms from four different (2,4-dichloro-phen-oxy)acetate ligands and two water mol-ecules, and displays a distorted square-anti-prismatic coordination geometry. Water 73-78 carbonic anhydrase 2 Homo sapiens 88-94 21202200-1 2008 In the title coordination polymer, {[Ca(C(8)H(5)Cl(2)O(3))(2)(H(2)O)(2)] H(2)O}(n), the Ca(II) atom is eight-coordinated by six O atoms from four different (2,4-dichloro-phen-oxy)acetate ligands and two water mol-ecules, and displays a distorted square-anti-prismatic coordination geometry. Water 203-208 carbonic anhydrase 2 Homo sapiens 88-94 18247480-2 2008 In contrast to the long-held conjecture in the experimental literature, the computed potentials of mean force (PMF) suggest that the proton transfer in CAII is not very sensitive to the orientation of the acceptor group (His 64) and, therefore, the number of water molecules that bridge the donor (zinc-water) and acceptor groups. Water 259-264 carbonic anhydrase 2 Homo sapiens 152-156 18247480-2 2008 In contrast to the long-held conjecture in the experimental literature, the computed potentials of mean force (PMF) suggest that the proton transfer in CAII is not very sensitive to the orientation of the acceptor group (His 64) and, therefore, the number of water molecules that bridge the donor (zinc-water) and acceptor groups. Water 303-308 carbonic anhydrase 2 Homo sapiens 152-156 18441928-5 2008 When the Ca2+ concentration of overlying water increased from 1 mmol/L to 5 mmol/L, the phosphorus concentration was reduced by about 36% in the 72nd day. Water 41-46 carbonic anhydrase 2 Homo sapiens 9-12 17083230-9 2006 The remaining four coordination sites on Ca(II) in 1 come from two coordinated water molecules and a chelating carboxylate bridging from an adjacent [Ca(PDA)(H2O)2].2H2O complex. Water 79-84 carbonic anhydrase 2 Homo sapiens 41-47 17506534-0 2007 pKa analysis for the zinc-bound water in human carbonic anhydrase II: Benchmark for "multiscale" QM/MM simulations and mechanistic implications. Water 32-37 carbonic anhydrase 2 Homo sapiens 47-68 17506534-3 2007 The pKa of the zinc-bound water, calculated with a SCC-DFTB/MM-GSBP based thermodynamic integration approach, agrees well with experiments for the wild type CAII. Water 26-31 carbonic anhydrase 2 Homo sapiens 157-161 17202139-9 2007 Based on these features, we suggest here a catalytic mechanism for hCAII: the tautomerization of His(64) can mediate the transfers of both protons and water molecules at a neutral pH with high efficiency, requiring no time- or energy-consuming processes. Water 151-156 carbonic anhydrase 2 Homo sapiens 67-72 17071654-1 2007 Small molecule rescue of mutant forms of human carbonic anhydrase II (HCA II) occurs by participation of exogenous donors/acceptors in the proton transfer pathway between the zinc-bound water and solution. Water 186-191 carbonic anhydrase 2 Homo sapiens 47-68 16807956-5 2006 The structures as determined by X-ray crystallography of the hCA II-l-His/d-His adducts showed the activators to be anchored at the entrance of the active site, contributing to extended networks of hydrogen bonds with amino acid residues/water molecules present in the cavity, explaining their different potency and interaction patterns with various isozymes. Water 238-243 carbonic anhydrase 2 Homo sapiens 61-67 16763307-2 2006 The Ca(II) cation, lying on a twofold axis, is coordinated by two water molecules and six malonate O atoms. Water 66-71 carbonic anhydrase 2 Homo sapiens 4-10 16557501-1 2006 We have investigated the possible proton transfer pathways from the surface of the protein to the zinc-bound water molecule in the mutant His-64-Ala of human carbonic anhydrase II. Water 109-114 carbonic anhydrase 2 Homo sapiens 158-179 16521550-0 2006 [Studies of interactions of carbonic anhydrase B with water and urea: II. Water 54-59 carbonic anhydrase 2 Homo sapiens 28-48 16214338-4 2005 The X-ray crystallographic structure of the hCA II-l-His adduct showed the activator to be anchored at the entrance of the active site cavity, participating in an extended network of hydrogen bonds with the amino acid residues His64, Asn67, and Gln92 and, with three water molecules connecting it to the zinc-bound water. Water 267-272 carbonic anhydrase 2 Homo sapiens 44-50 16214338-4 2005 The X-ray crystallographic structure of the hCA II-l-His adduct showed the activator to be anchored at the entrance of the active site cavity, participating in an extended network of hydrogen bonds with the amino acid residues His64, Asn67, and Gln92 and, with three water molecules connecting it to the zinc-bound water. Water 315-320 carbonic anhydrase 2 Homo sapiens 44-50 16212054-0 2005 [A study of interactions of carbonic anhydrase B with water and urea. Water 54-59 carbonic anhydrase 2 Homo sapiens 28-48 16212054-5 2005 We found out that native carbonic anhydrase B is able to form water-protein units that are probabilistically distributed with respect to their sizes. Water 62-67 carbonic anhydrase 2 Homo sapiens 25-45 15981579-0 2005 [Carbonic anhydrase B interactions with water and urea]. Water 40-45 carbonic anhydrase 2 Homo sapiens 1-21 14984209-1 2004 The hydration of CO2 catalyzed by human carbonic anhydrase II (HCA II) is accompanied by proton transfer from the zinc-bound water of the enzyme to solution. Water 125-130 carbonic anhydrase 2 Homo sapiens 40-61 15070393-3 2004 The accepted mechanism for CAII would predict that water would be bound to the Zn(2+) at pH 5 and hydroxide would be bound at pH 8.5. Water 51-56 carbonic anhydrase 2 Homo sapiens 27-31 16256541-3 2003 The presence of Mn(II) and Ca(II) ions alone led to a systematic reduction in zeta potential due to specific adsorption of positively charged metal ion-based hydrolysis products at the kaolinite-water interface. Water 195-200 carbonic anhydrase 2 Homo sapiens 27-33 12418662-4 2002 For the water sample whose adsorption capacity was least affected by Ca(II), the effect of pH was subsequently examined for four water pH levels (pH = 5.5-10) and these three ACs. Water 8-13 carbonic anhydrase 2 Homo sapiens 69-75 18968965-3 2003 The method was applied to the simultaneous determination of Na(I), Ca(II), Mg(II) and Zn(II) in drinking water with satisfactory results and a detection limit of 32 ng ml(-1) for Zn(II) was obtained. Water 105-110 carbonic anhydrase 2 Homo sapiens 67-73 12656477-1 2002 We have developed a versatile tool for the delivery of inhibitors of carbonic anhydrase II, which allows modification of a hydrophobic drug with either a water-solubilizing, photolabile cage or a hydrophobic, photolabile cage. Water 154-159 carbonic anhydrase 2 Homo sapiens 69-90 11863462-1 2002 The maximal velocity of catalysis of CO(2) hydration by human carbonic anhydrase II (HCA II) requires proton transfer from zinc-bound water to solution assisted by His 64. Water 134-139 carbonic anhydrase 2 Homo sapiens 62-83 11980488-9 2002 These results suggest that the proper organization of the hydrogen bond network within OEC for the water oxidation chemistry requires the Ca2+ ion and indicate that the role of Ca2+ is not purely structurally defined by the physical properties of the ion, such as valence and ionic radius. Water 99-104 carbonic anhydrase 2 Homo sapiens 138-141 11980488-9 2002 These results suggest that the proper organization of the hydrogen bond network within OEC for the water oxidation chemistry requires the Ca2+ ion and indicate that the role of Ca2+ is not purely structurally defined by the physical properties of the ion, such as valence and ionic radius. Water 99-104 carbonic anhydrase 2 Homo sapiens 177-180 11980488-10 2002 On the basis of these and other findings, we propose that Ca2+ is necessary for the formation of the hydrogen bond network that is involved in the reaction step of water oxidation. Water 164-169 carbonic anhydrase 2 Homo sapiens 58-61 11902785-3 2002 The compounds released metal cations (Mg2+, Ca2 , Fe3+) and/or their hydroxides responding to various water environments due to their buffering pH function. Water 102-107 carbonic anhydrase 2 Homo sapiens 44-47 11327835-1 2001 Histidine 64 in human carbonic anhydrase II (HCA II) functions in the catalytic pathway of CO(2) hydration as a shuttle to transfer protons between the zinc-bound water and bulk water. Water 163-168 carbonic anhydrase 2 Homo sapiens 22-43 11414818-1 2001 Catalysis of (18)O exchange between CO(2) and water catalyzed by a Co(II)-substituted mutant of human carbonic anhydrase II is analyzed to show the rate of release of H(2)(18)O from the active site. Water 46-51 carbonic anhydrase 2 Homo sapiens 102-123 11327835-1 2001 Histidine 64 in human carbonic anhydrase II (HCA II) functions in the catalytic pathway of CO(2) hydration as a shuttle to transfer protons between the zinc-bound water and bulk water. Water 178-183 carbonic anhydrase 2 Homo sapiens 22-43 9741850-7 1998 Mutations of various residues around the active site provide further insight into the corresponding experimental results and, in fact, suggest an important role for the solvent water molecules in the CA II catalytic mechanism. Water 177-182 carbonic anhydrase 2 Homo sapiens 200-205 11234387-1 2001 The interaction between carbonic anhydrase B in the molten globule state and water molecules was studied by high-resolution NMR spectroscopy. Water 77-82 carbonic anhydrase 2 Homo sapiens 24-44 11015219-4 2000 The second, low-occupancy form consists of a hCAII-cyanamide-water ternary complex where the catalytic zinc ion, still being bound to cyanamide, is approached by a water molecule in a five-coordinate adduct. Water 61-66 carbonic anhydrase 2 Homo sapiens 45-50 11015219-4 2000 The second, low-occupancy form consists of a hCAII-cyanamide-water ternary complex where the catalytic zinc ion, still being bound to cyanamide, is approached by a water molecule in a five-coordinate adduct. Water 164-169 carbonic anhydrase 2 Homo sapiens 45-50 10998050-6 2000 In a similar way to human carbonic anhydrase II, the buffer behaves formally as a second substrate in a ping-pong pattern, suggesting that proton transfer between a zinc-bound water molecule and buffer limits the maximal rate of catalysis in both systems at low buffer concentrations. Water 176-181 carbonic anhydrase 2 Homo sapiens 26-47 10975575-0 2000 Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Water 0-5 carbonic anhydrase 2 Homo sapiens 58-78 10961683-5 2000 On stabilisation of the water structure in the presence of low ethanol concentrations a stabilisation of the DNA macromolecule occurs that leads to the increase of the Ca2+ ion concentration necessary for DNA compactisation. Water 24-29 carbonic anhydrase 2 Homo sapiens 168-171 10961683-6 2000 Comparison of the effects of ethanol on Ca2+-induced structural transitions in DNA and polyphosphates in mixed solvents permits to suppose that at alcohol concentrations in solution resulting in disruption of the water spatial structure, some peculiarities are observed in the behavior of those molecules whose hydrophobic interactions are essential. Water 213-218 carbonic anhydrase 2 Homo sapiens 40-43 10550681-6 1999 Several hydrogen bonds involving active site residues Thr199 and Thr200 as well as three water molecules (Wat99, Wat122, and Wat123) further stabilize the urea-hCA II adduct. Water 89-94 carbonic anhydrase 2 Homo sapiens 160-166 8027057-1 1994 The catalysis of the hydration of CO2 by human carbonic anhydrase II (HCA II) includes the transfer of a proton from zinc-bound water to histidine 64 utilizing a network of intervening hydrogen-bonded water molecules, then the proton is transferred to buffer in solution. Water 128-133 carbonic anhydrase 2 Homo sapiens 47-68 9398308-6 1997 Metal geometry changes to trigonal bipyramidal in H119N CAII due to the addition of a second water molecule to the zinc coordination polyhedron and also in H94N CAII due to the displacement of zinc-bound hydroxide by the bidentate coordination of a Tris molecule. Water 93-98 carbonic anhydrase 2 Homo sapiens 56-60 8987973-4 1996 Furthermore, an alternative proton transfer pathway, consisting of an active site solvent-mediated proton transfer from zinc-water to imidazole buffer, is inhibited in the A65F, A65L, and A65H CAII variants. Water 125-130 carbonic anhydrase 2 Homo sapiens 193-197 8027057-1 1994 The catalysis of the hydration of CO2 by human carbonic anhydrase II (HCA II) includes the transfer of a proton from zinc-bound water to histidine 64 utilizing a network of intervening hydrogen-bonded water molecules, then the proton is transferred to buffer in solution. Water 201-206 carbonic anhydrase 2 Homo sapiens 47-68 8142888-0 1994 Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors. Water 32-37 carbonic anhydrase 2 Homo sapiens 47-68 8261139-8 1993 Upon reperfusion with normal artificial sea water, [Ca2+]i is elevated at the tip of the cut axon and a membrane seal is formed. Water 44-49 carbonic anhydrase 2 Homo sapiens 52-55 8771178-7 1995 In monoclinic H94D CAII, a fully occupied zinc ion is tetrahedrally coordinated by D94, H96, H119 and a water molecule. Water 104-109 carbonic anhydrase 2 Homo sapiens 19-23 1935176-4 1991 The competitive effect of Ca2+/trehalose is interpreted as a consequence of the different amount of interfacial water displaced by each compound in their adsorption on the water/lipid interface. Water 112-117 carbonic anhydrase 2 Homo sapiens 26-29 1935176-4 1991 The competitive effect of Ca2+/trehalose is interpreted as a consequence of the different amount of interfacial water displaced by each compound in their adsorption on the water/lipid interface. Water 172-177 carbonic anhydrase 2 Homo sapiens 26-29 1974931-3 1990 From computer graphics analysis and MD simulations on the zinc hydroxide form of human carbonic anhydrase II we find that this interaction forces the hydroxide hydrogen atom to be in a "down" position relative to the deep water-binding pocket. Water 222-227 carbonic anhydrase 2 Homo sapiens 87-108 34259506-0 2021 Spectrally Resolved Estimation of Water Entropy in the Active Site of Human Carbonic Anhydrase II. Water 34-39 carbonic anhydrase 2 Homo sapiens 76-97 34082230-5 2021 Pressure solution is promoted when the interfacial water layers of calcite remain undisturbed under stress (e.g. with Ca(II)) and the dissolved ions and water lubricate the interface - a phenomenon called pressure-solution facilitated slip. Water 51-56 carbonic anhydrase 2 Homo sapiens 118-124 34259506-3 2021 One example is human carbonic anhydrase II, whose active site harbors a conserved network of structural water molecules that are essential for enzymatic catalysis. Water 104-109 carbonic anhydrase 2 Homo sapiens 21-42 34259506-5 2021 Here, we use atomistic molecular dynamics simulations to compute the absolute entropy of the individual water molecules confined in the active site of hCAII using a spectrally resolved estimation (SRE) approach. Water 104-109 carbonic anhydrase 2 Homo sapiens 151-156 35140543-1 2022 With the solvothermal reactions of flexible tetracarboxylic acid ligand with the Cd(II) and Ca(II) ions, we acquired a new heterometallic coordination polymer formulated as {(Cd2Ca2(L)2(DMF)2(H2O)7) (DMF) 2(H2O)}n (1, H4L is 5-(bis(4-carboxybenzyl)amino)isophthalic acid, DMF is N,N"-Dimethylformamide). Water 192-195 carbonic anhydrase 2 Homo sapiens 92-98 35140543-1 2022 With the solvothermal reactions of flexible tetracarboxylic acid ligand with the Cd(II) and Ca(II) ions, we acquired a new heterometallic coordination polymer formulated as {(Cd2Ca2(L)2(DMF)2(H2O)7) (DMF) 2(H2O)}n (1, H4L is 5-(bis(4-carboxybenzyl)amino)isophthalic acid, DMF is N,N"-Dimethylformamide). Water 207-210 carbonic anhydrase 2 Homo sapiens 92-98 2851333-0 1988 Hydration of CO2 by carbonic anhydrase: intramolecular proton transfer between Zn2+-bound H2O and histidine 64 in human carbonic anhydrase II. Water 90-93 carbonic anhydrase 2 Homo sapiens 120-141 2501305-9 1989 These results support the proposal of Pocker and Janjic and the suggested role of histidine 64 in carbonic anhydrase II as a proton shuttle residue that transfers a proton from zinc-bound water to buffer in solution. Water 188-193 carbonic anhydrase 2 Homo sapiens 98-119 2851333-1 1988 The energy barrier for the intramolecular proton transfer between zinc-bound water and His 64 in the active site of human carbonic anhydrase II (HCA II) has been studied at the partial retention of diatomic differential overlap (PRDDO) level. Water 77-82 carbonic anhydrase 2 Homo sapiens 122-143 3488096-0 1986 Different receptor sites for Ca2+ and Na+ in single water fibers of the frog glossopharyngeal nerve. Water 52-57 carbonic anhydrase 2 Homo sapiens 29-32 3233597-5 1988 Spectroscopic and other evidence suggested that the Mg(II) ion in the Mg(D-glucose)X2.4 H2O adducts six-coordinate, binding to a D-glucose molecule (possibly via O-1 and O-2 atoms) and to four H2O molecules, whereas, in the corresponding 1:1 Ca-D-glucose adduct, the Ca(II) ion is possibly seven-coordinate, binding to a sugar moiety (through the O-1, O-2, and other sugar donor atoms) and to four H2O molecules. Water 88-91 carbonic anhydrase 2 Homo sapiens 267-273 3488096-5 1986 The selective elimination by the pronase E treatment indicates that there exist different receptor sites for Ca2+ and Na+ in single water fibers of the frog glossopharyngeal nerve. Water 132-137 carbonic anhydrase 2 Homo sapiens 109-112 6817788-1 1982 By measuring the rate of exchange at chemical equilibrium of 18O between HCO3- and H2O catalyzed by human carbonic anhydrase II in the absence of buffers, we have determined the rate of release from the enzyme of water bearing substrate oxygen. Water 83-86 carbonic anhydrase 2 Homo sapiens 106-127 6423238-8 1984 The effect caused by xylitol and sorbitol was explained in terms of partial displacement of water molecules in the primary hydration layer of Ca(II) ions, caused by competition between polyol and water molecules. Water 92-97 carbonic anhydrase 2 Homo sapiens 142-148 6423238-8 1984 The effect caused by xylitol and sorbitol was explained in terms of partial displacement of water molecules in the primary hydration layer of Ca(II) ions, caused by competition between polyol and water molecules. Water 196-201 carbonic anhydrase 2 Homo sapiens 142-148 6838201-6 1983 We find that sulfhydryl agents of which water-soluble mercurials were most effective induce Ca2+ release. Water 40-45 carbonic anhydrase 2 Homo sapiens 92-95 6817788-1 1982 By measuring the rate of exchange at chemical equilibrium of 18O between HCO3- and H2O catalyzed by human carbonic anhydrase II in the absence of buffers, we have determined the rate of release from the enzyme of water bearing substrate oxygen. Water 213-218 carbonic anhydrase 2 Homo sapiens 106-127 33916181-2 2021 The contrast agents showed MR relaxivities typical of gadolinium complexes with a single water molecule coordinated to a Gd3+ center (i.e., ~4.54 mM-1s-1) for both CA1 and CA2 at 60 MHz. Water 89-94 carbonic anhydrase 2 Homo sapiens 172-175 7284311-14 1981 For optimal binding in the absence of Ca2+, a long-distance hydrogen bond between these two residues is required; this can be established via a water molecule. Water 144-149 carbonic anhydrase 2 Homo sapiens 38-41 110618-0 1979 The water structure in the active cleft on human carbonic anhydrase B. Water 4-9 carbonic anhydrase 2 Homo sapiens 49-69 5483169-0 1970 Effect of Ca2+ on the water and non-electrolyte permeability of phospholipid membranes. Water 22-27 carbonic anhydrase 2 Homo sapiens 10-13 30802427-1 2019 Aquaporin 0 (AQP0) is essential for eye lens homeostasis as is regulation of its water permeability by Ca2+, which occurs through interactions with calmodulin (CaM), but the underlying molecular mechanisms are not well understood. Water 81-86 carbonic anhydrase 2 Homo sapiens 103-106 33585447-6 2020 Mitochondrial Ca2+ overload from the intracellular Ca2+-flux system located at the ER-mitochondrial axis can induce mitochondrial dilation during paraptosis, while the accumulation of misfolded proteins within the ER lumen is believed to exert an osmotic force and draw water from the cytoplasm to distend the ER lumen. Water 270-275 carbonic anhydrase 2 Homo sapiens 14-17 33585447-6 2020 Mitochondrial Ca2+ overload from the intracellular Ca2+-flux system located at the ER-mitochondrial axis can induce mitochondrial dilation during paraptosis, while the accumulation of misfolded proteins within the ER lumen is believed to exert an osmotic force and draw water from the cytoplasm to distend the ER lumen. Water 270-275 carbonic anhydrase 2 Homo sapiens 51-54 31268335-2 2019 In this essay, we prepared a new cluster-based CaII-MOFs {[Ca1.5(mu8-HL1)(DMF)2] DMF}n (1) with good water dispersibility, excellent photoluminescence properties (FL quantum yield of 20.37%) and great fluorescence stability. Water 101-106 carbonic anhydrase 2 Homo sapiens 47-51 30380445-1 2019 Carbonic anhydrase (CA) II plays major roles in pH regulation of body, protection of electrolyte balance, transportation of water and some metabolic pathways. Water 124-129 carbonic anhydrase 2 Homo sapiens 0-26 30089212-2 2018 In this study, via using the lipid bilayer as a soft substrate to accommodate the duplex oligonucleotide, the structure of the water layer surrounding the oligonucleotide was detected under the perturbation of the calcium ions (Ca2+) with chiral and achiral sum frequency generation (SFG) vibrational spectroscopy. Water 127-132 carbonic anhydrase 2 Homo sapiens 228-231 30089212-3 2018 With increasing Ca2+ concentration, both the chiral and achiral water vibrational signals had similar concentration-dependent changes, i.e., an initial decreasing phase followed by an increasing phase. Water 64-69 carbonic anhydrase 2 Homo sapiens 16-19 30188134-0 2018 Effects of Ca2+ Ion Condensation on the Molecular Structure of Polystyrene Sulfonate at Air-Water Interfaces. Water 92-97 carbonic anhydrase 2 Homo sapiens 11-14 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 114-119 carbonic anhydrase 2 Homo sapiens 16-37 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 114-119 carbonic anhydrase 2 Homo sapiens 39-43 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 114-119 carbonic anhydrase 2 Homo sapiens 128-132 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 161-164 carbonic anhydrase 2 Homo sapiens 16-37 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 161-164 carbonic anhydrase 2 Homo sapiens 39-43 29971013-12 2018 Recently, using carbonic anhydrase II (CAII)-filled erythrocyte vesicles, AQP1 has been demonstrated to transport water for the CAII-mediated reaction, CO2(g) + H2O HCO3-(aq) + H+(aq). Water 161-164 carbonic anhydrase 2 Homo sapiens 128-132 29729279-4 2018 Bovine and human CAII and CAIV have been reported to exert nitrite reductase and nitrous anhydride activity: 2 NO2- + 2 H+ [2 HONO] N2O3 + H2O. Water 143-146 carbonic anhydrase 2 Homo sapiens 17-21 29795045-4 2018 Our structural studies show that in hCA VII the network of ordered water molecules, which connects the zinc bound solvent molecule to the proton shuttle His64, is altered compared to hCA II, causing a reduction of the catalytic efficiency. Water 67-72 carbonic anhydrase 2 Homo sapiens 183-189 29729279-3 2018 Renal CAII and CAIV are involved in the reabsorption of nitrite, the autoxidation product of the signalling molecule nitric oxide (NO): 4 NO + O2 + 2 H2O 4 ONO- + 4 H+. Water 150-153 carbonic anhydrase 2 Homo sapiens 6-10 29354275-4 2018 The structures reveal new intermediate solvent states of hCA II that provide crystallographic snapshots during the restoration of the proton-transfer water network in the active site. Water 150-155 carbonic anhydrase 2 Homo sapiens 57-63 29429876-3 2018 We present room temperature neutron structures of hCA II in complex with three clinical drugs that provide in-depth analysis of drug binding, including protonation states of the inhibitors, hydration water structure, and direct visualization of hydrogen-bonding networks in the enzyme"s active site. Water 200-205 carbonic anhydrase 2 Homo sapiens 50-56 29266943-4 2018 In this study, X-ray crystallography showed acesulfame potassium (Ace K) binding directly to the catalytic zinc in CA IX (mimic) and through a bridging water in CA II. Water 152-157 carbonic anhydrase 2 Homo sapiens 161-166 29354275-8 2018 This study provides the first "physical" glimpse of how a water reservoir flows into the hCA II active site during its catalytic activity. Water 58-63 carbonic anhydrase 2 Homo sapiens 89-95 27789884-0 2016 Synthesis of [H22 Zr5 WO4 10 P2O7]n 26n H2O by response surface methodology to adsorb Ca(II) in manganiferous wastewater. Water 40-43 carbonic anhydrase 2 Homo sapiens 86-92 27789967-4 2016 METHODS: Free Ca2+ was measured with an ion-sensitive electrode in vitro in hard water (100-500 ppm, Ca2+) before and after addition of the cleanser and/or its components. Water 81-86 carbonic anhydrase 2 Homo sapiens 14-17 27789967-5 2016 In an exploratory study, absorption of Ca2+ into skin from hard water was determined in three female participants (aged 21-29 years). Water 64-69 carbonic anhydrase 2 Homo sapiens 39-42 27789967-8 2016 In the exploratory in vivo study, we measured a reduction of ~15% in free Ca2+ from simulated hard water over 10 minutes. Water 99-104 carbonic anhydrase 2 Homo sapiens 74-77 27789967-9 2016 CONCLUSION: Baby cleansers can bind free Ca2+ and reduce the effective water hardness of bath water. Water 71-76 carbonic anhydrase 2 Homo sapiens 41-44 27789967-9 2016 CONCLUSION: Baby cleansers can bind free Ca2+ and reduce the effective water hardness of bath water. Water 94-99 carbonic anhydrase 2 Homo sapiens 41-44 27789967-10 2016 Reducing the amount of free Ca2+ in the water will reduce the availability of the ion for binding to the skin. Water 40-45 carbonic anhydrase 2 Homo sapiens 28-31 27789967-11 2016 Altering or reducing free Ca2+ concentrations in bath water may be an important parameter in creating the ideal baby bath. Water 54-59 carbonic anhydrase 2 Homo sapiens 26-29 25902526-1 2015 Human carbonic anhydrase II (HCA II) uses a Zn-bound OH(-)/H2O mechanism to catalyze the reversible hydration of CO2. Water 59-62 carbonic anhydrase 2 Homo sapiens 6-27 26592023-4 2015 Therefore, some measures are necessary to avoid precipitation, including: (1) raw water pretreatment to reduce the concentrations of Ca2 and Mg2. Water 82-87 carbonic anhydrase 2 Homo sapiens 133-136 25463674-1 2014 Here, we used a strategy to answer to the question that whether Ca(II) ion is specific for water oxidation or not? Water 91-96 carbonic anhydrase 2 Homo sapiens 64-70 25738615-1 2015 This paper uses the binding pocket of human carbonic anhydrase II (HCAII, EC 4.2.1.1) as a tool to examine the properties of Hofmeister anions that determine (i) where, and how strongly, they associate with concavities on the surfaces of proteins and (ii) how, upon binding, they alter the structure of water within those concavities. Water 303-308 carbonic anhydrase 2 Homo sapiens 44-65 25463674-3 2014 We proposed that Ca(II), K(I), Mg(II), La(III) and Ni(II), between layers are important to form efficient water-oxidizing catalyst, but not specific in water oxidation. Water 106-111 carbonic anhydrase 2 Homo sapiens 17-23 25463674-3 2014 We proposed that Ca(II), K(I), Mg(II), La(III) and Ni(II), between layers are important to form efficient water-oxidizing catalyst, but not specific in water oxidation. Water 152-157 carbonic anhydrase 2 Homo sapiens 17-23 25317482-1 2014 A novel noncentrosymmetric calcium borate, Ca2[B5O9] (OH) H2O (1), was synthesized under solvothermal condition using mixed solvents of pyridine and H2O. Water 58-61 carbonic anhydrase 2 Homo sapiens 43-46 28811451-1 2013 A novel Ca(II) coordination polymer, [CaL(4,4"-bipyridyl)(H2O)4]n (L = 1,6-naphthalenedisulfonate), was synthesized by reaction of calcium perchlorate with 1,6-naphthalenedisulfonic acid disodium salt and 4,4"-bipyridyl in CH3CH2OH/H2O. Water 58-61 carbonic anhydrase 2 Homo sapiens 8-13 25580212-2 2014 Several mechanistic proposals describe the unique manganese center as a site for water binding and subsequent formation of a high valent Mn-oxo center that reacts with a M-OH unit (M = Mn or CaII) to form the O-O bond. Water 81-86 carbonic anhydrase 2 Homo sapiens 191-195 28811451-4 2013 The geometry of the Ca(II) ion is a distorted CaNO6 pengonal bipyramid, arising from its coordination by four water molecules, one nitrogen atom of 4,4"-bipyridyl molecule, and two oxygen atoms from two L ligands. Water 110-115 carbonic anhydrase 2 Homo sapiens 20-26 23274254-0 2013 A vibrational spectroscopic study of the phosphate mineral zanazziite - Ca2(MgFe2+)(MgFe2+Al)4Be4(PO4)6.6(H2O). Water 106-109 carbonic anhydrase 2 Homo sapiens 72-75 23633596-5 2013 However, addition of GOL does affect the kinetics of CA II, presumably as it displaces the water proton-transfer network in the active site. Water 91-96 carbonic anhydrase 2 Homo sapiens 53-58 23232865-4 2013 The first solvation shell of Ca(II) is formed by six water molecules, while the second shell contains five. Water 53-58 carbonic anhydrase 2 Homo sapiens 29-35 23452087-10 2013 In conclusion, MDPT was found to be a water-soluble chelator showing a clear preference to soft/borderline metal-ions and a remarkable selectivity to those metal-ions vs Ca(II) ions. Water 38-43 carbonic anhydrase 2 Homo sapiens 170-176 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 153-159 carbonic anhydrase 2 Homo sapiens 124-130 23215152-0 2013 Water networks in fast proton transfer during catalysis by human carbonic anhydrase II. Water 0-5 carbonic anhydrase 2 Homo sapiens 65-86 23215152-1 2013 Variants of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with water molecules in the active-site cavity have provided insights into the proton transfer rates in this protein environment. Water 106-111 carbonic anhydrase 2 Homo sapiens 18-39 22878862-1 2013 We present molecular modeling of the structure and possible proton transfer pathways from the surface of the protein to the zinc-bound water molecule in the active site of the mutant His-107-Tyr of human carbonic anhydrase II (HCAII). Water 135-140 carbonic anhydrase 2 Homo sapiens 204-225 22998407-2 2012 The conversion of water to dioxygen in photosynthesis illustrates one example, in which a redox-inactive Ca(II) ion and four manganese ions are required for function. Water 18-23 carbonic anhydrase 2 Homo sapiens 105-111 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 0-5 carbonic anhydrase 2 Homo sapiens 124-130 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 0-5 carbonic anhydrase 2 Homo sapiens 159-165 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 69-75 carbonic anhydrase 2 Homo sapiens 124-130 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 69-75 carbonic anhydrase 2 Homo sapiens 159-165 22998407-8 2012 [Co(II)MST(OH(2))](-) was oxidized to form [Co(III)MST(OH(2))] that was further converted to [Co(III)MST(mu-OH)Ca(II) 15-crown-5](+) ([Co(III)(mu-OH)Ca(II)](+)) in the presence of base and Ca(II)OTf(2)/15-crown-5. Water 11-17 carbonic anhydrase 2 Homo sapiens 111-117 22998407-8 2012 [Co(II)MST(OH(2))](-) was oxidized to form [Co(III)MST(OH(2))] that was further converted to [Co(III)MST(mu-OH)Ca(II) 15-crown-5](+) ([Co(III)(mu-OH)Ca(II)](+)) in the presence of base and Ca(II)OTf(2)/15-crown-5. Water 11-17 carbonic anhydrase 2 Homo sapiens 149-155 22998407-8 2012 [Co(II)MST(OH(2))](-) was oxidized to form [Co(III)MST(OH(2))] that was further converted to [Co(III)MST(mu-OH)Ca(II) 15-crown-5](+) ([Co(III)(mu-OH)Ca(II)](+)) in the presence of base and Ca(II)OTf(2)/15-crown-5. Water 55-61 carbonic anhydrase 2 Homo sapiens 111-117 22998407-8 2012 [Co(II)MST(OH(2))](-) was oxidized to form [Co(III)MST(OH(2))] that was further converted to [Co(III)MST(mu-OH)Ca(II) 15-crown-5](+) ([Co(III)(mu-OH)Ca(II)](+)) in the presence of base and Ca(II)OTf(2)/15-crown-5. Water 55-61 carbonic anhydrase 2 Homo sapiens 149-155 22732064-1 2012 Deprotonation of zinc-bound water in carbonic anhydrase II is the rate-limiting step in the catalysis of carbon dioxide between gas- and water-soluble forms. Water 28-33 carbonic anhydrase 2 Homo sapiens 37-58 22732064-1 2012 Deprotonation of zinc-bound water in carbonic anhydrase II is the rate-limiting step in the catalysis of carbon dioxide between gas- and water-soluble forms. Water 137-142 carbonic anhydrase 2 Homo sapiens 37-58