PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26197052-2 2015 Recently, we characterized a ditryptophan cross-link produced by the recombination of hSOD1-tryptophanyl radicals generated from attack of the carbonate radical produced during the bicarbonate-dependent peroxidase activity of the enzyme. Bicarbonates 181-192 superoxide dismutase 1 Homo sapiens 86-91 31102971-1 2019 Carbonate radicals (CO3-) are generated by the bicarbonate-dependent peroxidase activity of cytosolic superoxide dismutase (Cu,Zn-SOD, SOD-1). Bicarbonates 47-58 superoxide dismutase 1 Homo sapiens 135-140 31102971-5 2019 Solutions containing PGR (5-200 muM), SOD-1 (0.3-3 muM), H2O2 (2 mM) in bicarbonate buffer (200 mM, pH 7.4) showed a rapid loss of the PGR absorption band centered at 540 nm. Bicarbonates 72-83 superoxide dismutase 1 Homo sapiens 38-54 25237191-3 2014 The bicarbonate-dependent peroxidase activity of hSOD1 causes oxidation of its own solvent-exposed Trp(32) residue. Bicarbonates 4-15 superoxide dismutase 1 Homo sapiens 49-54 25237191-4 2014 The resulting products are apparently different from those produced in the absence of bicarbonate and are most likely specific for simian SOD1s, which contain the Trp(32) residue. Bicarbonates 86-97 superoxide dismutase 1 Homo sapiens 138-142 25237191-5 2014 The aims of this work were to examine whether the bicarbonate-dependent peroxidase activity of hSOD1 (hSOD1(WT) and hSOD1(G93A) mutant) triggers aggregation of the enzyme and to comprehend the role of the Trp(32) residue in the process. Bicarbonates 50-61 superoxide dismutase 1 Homo sapiens 95-100 25237191-5 2014 The aims of this work were to examine whether the bicarbonate-dependent peroxidase activity of hSOD1 (hSOD1(WT) and hSOD1(G93A) mutant) triggers aggregation of the enzyme and to comprehend the role of the Trp(32) residue in the process. Bicarbonates 50-61 superoxide dismutase 1 Homo sapiens 102-107 25237191-5 2014 The aims of this work were to examine whether the bicarbonate-dependent peroxidase activity of hSOD1 (hSOD1(WT) and hSOD1(G93A) mutant) triggers aggregation of the enzyme and to comprehend the role of the Trp(32) residue in the process. Bicarbonates 50-61 superoxide dismutase 1 Homo sapiens 126-134 23855710-4 2013 The chosen oxidizing system was the bicarbonate-dependent peroxidase activity of hSOD1 that consumes H2O2 to produce carbonate radical, which oxidizes the enzyme. Bicarbonates 36-47 superoxide dismutase 1 Homo sapiens 81-86 23855710-10 2013 Tempol consumption by the bicarbonate-dependent peroxidase activity of hSOD1 may be one of the reasons why high doses of tempol were required to afford protection in an ALS rat model. Bicarbonates 26-37 superoxide dismutase 1 Homo sapiens 71-76 19286663-5 2009 In view of recent observations, we hypothesized that the SOD1 peroxidase cycle relies on two steps: 1) reduction of SOD-Cu(II) by hydrogen peroxide followed by 2) oxidation of SOD-Cu(I) by peroxymonocarbonate, the product of the spontaneous reaction of bicarbonate with hydrogen peroxide, to produce SOD-Cu(II) and carbonate radical anion. Bicarbonates 253-264 superoxide dismutase 1 Homo sapiens 57-61 23003200-2 2012 CO(3)( -), generated in vitro by the SOD1/H(2)O(2)/bicarbonate system, readily promoted TMP, which was dependent on alpha-tocopherol and bicarbonate concentrations, and was inhibited by the CO(3)( -) scavenger ethanol; moreover, TMP induced in vitro by the SOD1/H(2)O(2)/bicarbonate system occurred in the presence of alpha-tocopherol that typically underwent slow oxidative consumption. Bicarbonates 137-148 superoxide dismutase 1 Homo sapiens 37-41 23003200-2 2012 CO(3)( -), generated in vitro by the SOD1/H(2)O(2)/bicarbonate system, readily promoted TMP, which was dependent on alpha-tocopherol and bicarbonate concentrations, and was inhibited by the CO(3)( -) scavenger ethanol; moreover, TMP induced in vitro by the SOD1/H(2)O(2)/bicarbonate system occurred in the presence of alpha-tocopherol that typically underwent slow oxidative consumption. Bicarbonates 137-148 superoxide dismutase 1 Homo sapiens 37-41 23003200-2 2012 CO(3)( -), generated in vitro by the SOD1/H(2)O(2)/bicarbonate system, readily promoted TMP, which was dependent on alpha-tocopherol and bicarbonate concentrations, and was inhibited by the CO(3)( -) scavenger ethanol; moreover, TMP induced in vitro by the SOD1/H(2)O(2)/bicarbonate system occurred in the presence of alpha-tocopherol that typically underwent slow oxidative consumption. Bicarbonates 51-62 superoxide dismutase 1 Homo sapiens 37-41 22984565-6 2012 Here, we provide direct structural evidence, from a 2.15 A resolution crystal structure, of (bi)carbonate captured at the active site of reduced SOD, consistent with the view that a bound carbonate intermediate could be formed, producing a diffusible carbonate radical upon reoxidation of copper. Bicarbonates 92-105 superoxide dismutase 1 Homo sapiens 145-148 20600836-0 2010 A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity. Bicarbonates 114-125 superoxide dismutase 1 Homo sapiens 80-102 20600836-3 2010 For instance, the antioxidant enzyme human superoxide dismutase 1 (hSod1) has been reported to undergo non-disulfide covalent dimerization and further oligomerization during its bicarbonate-dependent peroxidase activity. Bicarbonates 178-189 superoxide dismutase 1 Homo sapiens 43-65 20600836-3 2010 For instance, the antioxidant enzyme human superoxide dismutase 1 (hSod1) has been reported to undergo non-disulfide covalent dimerization and further oligomerization during its bicarbonate-dependent peroxidase activity. Bicarbonates 178-189 superoxide dismutase 1 Homo sapiens 67-72 16511360-4 2006 Enormous increase by bicarbonate in the rate of DCFH(2) oxidation distinguished CuZnSOD from cytochrome c and HRP. Bicarbonates 21-32 superoxide dismutase 1 Homo sapiens 80-87 18764780-6 2009 In the presence of (bi)carbonate and DTPA (diethylenetriaminepenta-acetic acid) (to suppress copper chemistry), CO(*-) produced distinct radical sites in both SOD1 and HSA, which caused protein aggregation without causing protein fragmentation. Bicarbonates 19-32 superoxide dismutase 1 Homo sapiens 159-163 18764780-8 2009 Finally, we propose a biochemical mechanism to explain CO(*-) production from CO2, enhanced protein radical formation and protection by (bi)carbonate against H2O2-induced fragmentation of the SOD1 active site. Bicarbonates 136-149 superoxide dismutase 1 Homo sapiens 192-196 19243126-3 2009 Among these, the ability of Sod1 to function as a peroxidase may be particularly relevant because it is increased in bicarbonate buffer and produces the reactive carbonate radical. Bicarbonates 117-128 superoxide dismutase 1 Homo sapiens 28-32 19243126-5 2009 To address this question, we systematically studied hSod1 peroxidase activity in the presence of nitrite, formate, and bicarbonate-carbon dioxide. Bicarbonates 119-130 superoxide dismutase 1 Homo sapiens 52-57 19243126-6 2009 Kinetic analyses of hydrogen peroxide consumption and of nitrite, formate, and bicarbonate-carbon dioxide oxidation showed that the Sod1-bound hydroxyl-like oxidant functions in the presence of nitrite and formate. Bicarbonates 79-90 superoxide dismutase 1 Homo sapiens 132-136 19243126-12 2009 In the presence of bicarbonate-carbon dioxide, sustained hSod1-mediated oxidations occurred with low steady-state concentrations of hydrogen peroxide (4-10 microM). Bicarbonates 19-30 superoxide dismutase 1 Homo sapiens 57-62 15777089-6 2005 On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions. Bicarbonates 162-166 superoxide dismutase 1 Homo sapiens 85-89 15777089-1 2005 Here, we investigated the effect of bicarbonate anion (HCO3-) on the peroxidase activity stimulated by the thiol oxidase activity of copper, zinc superoxide dismutase (SOD1) using electron spin resonance (ESR) and optical techniques. Bicarbonates 36-53 superoxide dismutase 1 Homo sapiens 168-172 15777089-6 2005 On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions. Bicarbonates 211-215 superoxide dismutase 1 Homo sapiens 85-89 15777089-1 2005 Here, we investigated the effect of bicarbonate anion (HCO3-) on the peroxidase activity stimulated by the thiol oxidase activity of copper, zinc superoxide dismutase (SOD1) using electron spin resonance (ESR) and optical techniques. Bicarbonates 55-59 superoxide dismutase 1 Homo sapiens 168-172 15777089-6 2005 On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions. Bicarbonates 211-215 superoxide dismutase 1 Homo sapiens 201-205 15777089-3 2005 The addition of HCO3- to aerobic incubations containing SOD1, Cys, and DTPA in phosphate buffer enhanced the peroxidase activity of SOD1, as measured by hydroxylation of cyclic nitrone spin traps, dichlorodihydrofluorescein oxidation to dichlorofluorescein, and oxidation of tyrosine to dityrosine. Bicarbonates 16-20 superoxide dismutase 1 Homo sapiens 56-60 15777089-3 2005 The addition of HCO3- to aerobic incubations containing SOD1, Cys, and DTPA in phosphate buffer enhanced the peroxidase activity of SOD1, as measured by hydroxylation of cyclic nitrone spin traps, dichlorodihydrofluorescein oxidation to dichlorofluorescein, and oxidation of tyrosine to dityrosine. Bicarbonates 16-20 superoxide dismutase 1 Homo sapiens 132-136 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Bicarbonates 97-110 superoxide dismutase 1 Homo sapiens 61-65 15777089-4 2005 The addition of catalase inhibited the SOD1 peroxidase activity stimulated by the thiol oxidase actvity, implicating an intermediary role for H2O2 in SOD1/Cys/HCO3(-)-mediated oxidation and hydroxylation reactions. Bicarbonates 159-163 superoxide dismutase 1 Homo sapiens 39-43 15777089-5 2005 Using a competitive kinetic method, rate constants for the reaction between the oxidant formed in the SOD1/Cys/HCO3- system and selected inhibitors were measured. Bicarbonates 111-115 superoxide dismutase 1 Homo sapiens 102-106 15607903-2 2005 These radicals are involved in H2O2-induced structural and functional damage to SOD1, and their mechanism of generation depends on copper and/or (bi)carbonate (i.e., CO2, CO3(-2), or HCO3-). Bicarbonates 145-158 superoxide dismutase 1 Homo sapiens 80-84 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Bicarbonates 97-110 superoxide dismutase 1 Homo sapiens 153-157 15607903-2 2005 These radicals are involved in H2O2-induced structural and functional damage to SOD1, and their mechanism of generation depends on copper and/or (bi)carbonate (i.e., CO2, CO3(-2), or HCO3-). Bicarbonates 183-188 superoxide dismutase 1 Homo sapiens 80-84 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Bicarbonates 97-110 superoxide dismutase 1 Homo sapiens 153-157 15607903-8 2005 In addition, (bi)carbonate enhanced H2O2-induced SOD1 turnover as demonstrated by an enhancement in oxygen evolution and SOD1 inactivation. Bicarbonates 13-26 superoxide dismutase 1 Homo sapiens 49-53 15607903-8 2005 In addition, (bi)carbonate enhanced H2O2-induced SOD1 turnover as demonstrated by an enhancement in oxygen evolution and SOD1 inactivation. Bicarbonates 13-26 superoxide dismutase 1 Homo sapiens 121-125 15544920-1 2004 Previously, we showed that oxidation of tryptophan-32 (Trp-32) residue was crucial for H(2)O(2)/bicarbonate (HCO(3)(-))-dependent covalent aggregation of human Cu,Zn SOD1 (hSOD1). Bicarbonates 96-107 superoxide dismutase 1 Homo sapiens 166-170 15544920-1 2004 Previously, we showed that oxidation of tryptophan-32 (Trp-32) residue was crucial for H(2)O(2)/bicarbonate (HCO(3)(-))-dependent covalent aggregation of human Cu,Zn SOD1 (hSOD1). Bicarbonates 96-107 superoxide dismutase 1 Homo sapiens 172-177 15123612-4 2004 However, HCO(3)(-) induced a Trp-32-derived radical from WT hSOD1 but not from bSOD1. Bicarbonates 9-15 superoxide dismutase 1 Homo sapiens 60-65 12686560-0 2003 Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products. Bicarbonates 0-11 superoxide dismutase 1 Homo sapiens 51-77 15135171-2 2004 Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3*-), a potent and selective oxidant. Bicarbonates 0-17 superoxide dismutase 1 Homo sapiens 63-68 15135171-2 2004 Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3*-), a potent and selective oxidant. Bicarbonates 0-17 superoxide dismutase 1 Homo sapiens 64-68 15135171-2 2004 Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3*-), a potent and selective oxidant. Bicarbonates 19-24 superoxide dismutase 1 Homo sapiens 63-68 15135171-2 2004 Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3*-), a potent and selective oxidant. Bicarbonates 19-24 superoxide dismutase 1 Homo sapiens 64-68 15135181-1 2004 At pH 7.4, CO2, rather than HCO3-, markedly enhances the oxidation of diverse substrates by SOD1 plus H2O2. Bicarbonates 28-32 superoxide dismutase 1 Homo sapiens 92-96 15135181-2 2004 Since the concentration of CO2 would fall with rising pH in HCO3- buffers, it was of interest to explore the effects of pH on the peroxidase activity of SOD1 in the presence and in the absence of HCO3-. Bicarbonates 60-64 superoxide dismutase 1 Homo sapiens 153-157 14717588-0 2004 Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Bicarbonates 114-125 superoxide dismutase 1 Homo sapiens 68-94 14717588-2 2004 The mechanism by which Cu,Zn-SOD/hydrogen peroxide/bicarbonate is able to oxidize substrates has been proposed to be dependent on an oxidant whose nature, diffusible carbonate radical anion or enzyme-bound peroxycarbonate, remains debatable. Bicarbonates 51-62 superoxide dismutase 1 Homo sapiens 23-32 14717588-9 2004 Overall, the results prove the diffusible and radical nature of the oxidants produced during the peroxidase activity of Cu,Zn-SOD in the presence of bicarbonate or nitrite. Bicarbonates 149-160 superoxide dismutase 1 Homo sapiens 120-129 12686560-11 2003 Molecular oxygen was needed for HCO3-/H2O2-dependent aggregation of hSOD1WT, implicating a role for a Trp-32-dependent peroxidative reaction in the covalent aggregation of hSOD1WT. Bicarbonates 32-36 superoxide dismutase 1 Homo sapiens 68-73 12686560-11 2003 Molecular oxygen was needed for HCO3-/H2O2-dependent aggregation of hSOD1WT, implicating a role for a Trp-32-dependent peroxidative reaction in the covalent aggregation of hSOD1WT. Bicarbonates 32-36 superoxide dismutase 1 Homo sapiens 68-75 12686560-13 2003 Implications of HCO3--dependent SOD1 peroxidase activity in amyotrophic lateral sclerosis disease are discussed. Bicarbonates 16-20 superoxide dismutase 1 Homo sapiens 32-36 15135181-2 2004 Since the concentration of CO2 would fall with rising pH in HCO3- buffers, it was of interest to explore the effects of pH on the peroxidase activity of SOD1 in the presence and in the absence of HCO3-. Bicarbonates 196-200 superoxide dismutase 1 Homo sapiens 153-157 12686560-1 2003 This study addresses the mechanism of covalent aggregation of human Cu,Zn-superoxide dismutase (hSOD1WT) induced by bicarbonate (HCO3-)-mediated peroxidase activity. Bicarbonates 116-127 superoxide dismutase 1 Homo sapiens 68-94 12686560-1 2003 This study addresses the mechanism of covalent aggregation of human Cu,Zn-superoxide dismutase (hSOD1WT) induced by bicarbonate (HCO3-)-mediated peroxidase activity. Bicarbonates 116-127 superoxide dismutase 1 Homo sapiens 96-103 12686560-1 2003 This study addresses the mechanism of covalent aggregation of human Cu,Zn-superoxide dismutase (hSOD1WT) induced by bicarbonate (HCO3-)-mediated peroxidase activity. Bicarbonates 129-134 superoxide dismutase 1 Homo sapiens 68-94 12686560-1 2003 This study addresses the mechanism of covalent aggregation of human Cu,Zn-superoxide dismutase (hSOD1WT) induced by bicarbonate (HCO3-)-mediated peroxidase activity. Bicarbonates 129-134 superoxide dismutase 1 Homo sapiens 96-103 12686560-2 2003 Higher molecular weight species (apparent dimers and trimers) of hSOD1WT were formed from incubation mixtures containing hSOD1WT, H2O2, and HCO3-. Bicarbonates 140-145 superoxide dismutase 1 Homo sapiens 65-70 12686560-2 2003 Higher molecular weight species (apparent dimers and trimers) of hSOD1WT were formed from incubation mixtures containing hSOD1WT, H2O2, and HCO3-. Bicarbonates 140-145 superoxide dismutase 1 Homo sapiens 65-72 12686560-3 2003 HCO3--dependent peroxidase activity and covalent aggregation of hSOD1WT were mimicked by UV photolysis of hSOD1-WT in the presence of a [Co(NH3)5CO3]+ complex that generates the carbonate radical anion (CO3.). Bicarbonates 0-4 superoxide dismutase 1 Homo sapiens 64-69 12686560-3 2003 HCO3--dependent peroxidase activity and covalent aggregation of hSOD1WT were mimicked by UV photolysis of hSOD1-WT in the presence of a [Co(NH3)5CO3]+ complex that generates the carbonate radical anion (CO3.). Bicarbonates 0-4 superoxide dismutase 1 Homo sapiens 106-111 11461912-9 2001 Cu,Zn-SOD plus H(2)O(2) caused the HCO(3)(-)-dependent oxidation of DCF, casting doubt on the validity of using DCF oxidation as a reliable measure of intracellular H(2)O(2) production. Bicarbonates 35-44 superoxide dismutase 1 Homo sapiens 6-9 12649272-4 2003 Here, we show that bicarbonate also substantially enhances the rate of self-inactivation of human wild type SOD1. Bicarbonates 19-30 superoxide dismutase 1 Homo sapiens 108-112 12649272-5 2003 Together, these observations suggest that the strong oxidant formed by hydrogen peroxide and SOD1 in the presence of bicarbonate arises from a pathway mechanistically distinct from that producing the oxidant in its absence. Bicarbonates 117-128 superoxide dismutase 1 Homo sapiens 93-97 12649272-7 2003 The 1.4 A resolution crystal structure of pathogenic SOD1 mutant D125H reveals the mode of oxyanion binding in the active site channel and implies that phosphate anion attenuates the bicarbonate effect by competing for binding to this site. Bicarbonates 183-194 superoxide dismutase 1 Homo sapiens 53-57 10497178-2 1999 We examined the effect of bicarbonate on the peroxidase activity of copper-zinc superoxide dismutase (SOD1), using the nitrite anion as a peroxidase probe. Bicarbonates 26-37 superoxide dismutase 1 Homo sapiens 102-106 10799477-2 2000 The effect of bicarbonate anion (HCO(3)(-)) on the peroxidase activity of copper, zinc superoxide dismutase (SOD1) was investigated using three structurally different probes: 5, 5"-dimethyl-1-pyrroline N-oxide (DMPO), tyrosine, and 2, 2"-azino-bis-[3-ethylbenzothiazoline]-6-sulfonic acid (ABTS). Bicarbonates 14-31 superoxide dismutase 1 Homo sapiens 109-113 10799477-2 2000 The effect of bicarbonate anion (HCO(3)(-)) on the peroxidase activity of copper, zinc superoxide dismutase (SOD1) was investigated using three structurally different probes: 5, 5"-dimethyl-1-pyrroline N-oxide (DMPO), tyrosine, and 2, 2"-azino-bis-[3-ethylbenzothiazoline]-6-sulfonic acid (ABTS). Bicarbonates 33-39 superoxide dismutase 1 Homo sapiens 109-113 10799477-6 2000 We postulate that HCO(3)(-) enhances SOD1 peroxidase activity via formation of a putative carbonate radical anion. Bicarbonates 18-27 superoxide dismutase 1 Homo sapiens 37-41 10799477-7 2000 This new and different perspective on HCO(3)(-)-mediated oxidative reactions of SOD1 may help us understand the free radical mechanism of SOD1 and related mutants linked to amyotrophic lateral sclerosis. Bicarbonates 38-45 superoxide dismutase 1 Homo sapiens 80-84 10799477-7 2000 This new and different perspective on HCO(3)(-)-mediated oxidative reactions of SOD1 may help us understand the free radical mechanism of SOD1 and related mutants linked to amyotrophic lateral sclerosis. Bicarbonates 38-45 superoxide dismutase 1 Homo sapiens 138-142 10940382-6 2000 Bicarbonate retarded formation of ONOO-, suggesting that .NO competes with bicarbonate for the oxidant SOD-Cu2+-.OH. Bicarbonates 0-11 superoxide dismutase 1 Homo sapiens 103-106 10940382-6 2000 Bicarbonate retarded formation of ONOO-, suggesting that .NO competes with bicarbonate for the oxidant SOD-Cu2+-.OH. Bicarbonates 75-86 superoxide dismutase 1 Homo sapiens 103-106 10641739-0 1999 On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase. Bicarbonates 15-26 superoxide dismutase 1 Homo sapiens 57-83 10497178-5 1999 However, bicarbonate enhanced SOD1/H(2)O(2)-dependent oxidation of tocopherols in the presence and absence of nitrite and dramatically enhanced SOD1/H(2)O(2)-mediated oxidation of unsaturated lipid in the presence of nitrite. Bicarbonates 9-20 superoxide dismutase 1 Homo sapiens 30-34 10497178-5 1999 However, bicarbonate enhanced SOD1/H(2)O(2)-dependent oxidation of tocopherols in the presence and absence of nitrite and dramatically enhanced SOD1/H(2)O(2)-mediated oxidation of unsaturated lipid in the presence of nitrite. Bicarbonates 9-20 superoxide dismutase 1 Homo sapiens 144-148 10497178-6 1999 These results, coupled with the finding that bicarbonate protects against inactivation of SOD1 by H(2)O(2), suggest that SOD1/H(2)O(2) oxidizes the bicarbonate anion to the carbonate radical anion. Bicarbonates 148-159 superoxide dismutase 1 Homo sapiens 90-94 10497178-6 1999 These results, coupled with the finding that bicarbonate protects against inactivation of SOD1 by H(2)O(2), suggest that SOD1/H(2)O(2) oxidizes the bicarbonate anion to the carbonate radical anion. Bicarbonates 148-159 superoxide dismutase 1 Homo sapiens 121-125 10497178-7 1999 Thus, the amplification of peroxidase activity of SOD1/H(2)O(2) by bicarbonate is attributed to the intermediary role of the diffusible oxidant, the carbonate radical anion. Bicarbonates 67-78 superoxide dismutase 1 Homo sapiens 50-54 10497178-11 1999 However, bicarbonate enhanced the peroxidase activity of SOD1 via formation of a putative carbonate radical anion. Bicarbonates 9-20 superoxide dismutase 1 Homo sapiens 57-61 10497178-6 1999 These results, coupled with the finding that bicarbonate protects against inactivation of SOD1 by H(2)O(2), suggest that SOD1/H(2)O(2) oxidizes the bicarbonate anion to the carbonate radical anion. Bicarbonates 45-56 superoxide dismutase 1 Homo sapiens 90-94 10497178-6 1999 These results, coupled with the finding that bicarbonate protects against inactivation of SOD1 by H(2)O(2), suggest that SOD1/H(2)O(2) oxidizes the bicarbonate anion to the carbonate radical anion. Bicarbonates 45-56 superoxide dismutase 1 Homo sapiens 121-125 9331967-3 1997 The inhibition constants Ki for SOD and its conjugate (SOD-catalase)mic in 0.1 M bicarbonate buffer, pH 10.2, were 0.1 and 0.25 microM, respectively. Bicarbonates 81-92 superoxide dismutase 1 Homo sapiens 32-35 9331967-1 1997 The catalytic activity of superoxide dismutase (SOD) and its conjugates with catalase and polymer peroxidase (p-peroxidase) obtained during covalent binding of enzymes with aldehyde dextrans was indirectly characterized by inhibition of adrenaline autoxidation in 0.1 M bicarbonate buffer, pH 10.2, and in microemulsion of 0.1 M aerosol OT (AOT) and Triton X-45 in octane containing 15% aqueous phase. Bicarbonates 270-281 superoxide dismutase 1 Homo sapiens 26-46 9880490-6 1999 The results indicate that HCO3- competes with other anions for the anion-binding site of SOD1 (Arg141) but does not bind directly to the copper. Bicarbonates 26-30 superoxide dismutase 1 Homo sapiens 89-93 9880490-10 1999 Thus, SOD1 acquires peroxidase activity at physiological pH only in the presence of HCO3- or structurally similar anions. Bicarbonates 84-88 superoxide dismutase 1 Homo sapiens 6-10 9880490-11 1999 Alterations in pH that shift the HCO3-/CO2 equilibrium as occur in disease processes such as ischemia, sepsis, or shock would modulate the peroxidase function of SOD1. Bicarbonates 33-37 superoxide dismutase 1 Homo sapiens 162-166 9618471-5 1998 The reaction of the WT SOD with H217O2 in bicarbonate/CO2 buffer yielded 63% DMPO/.17OH and 37% DMPO/.16OH. Bicarbonates 42-53 superoxide dismutase 1 Homo sapiens 23-26 9331967-1 1997 The catalytic activity of superoxide dismutase (SOD) and its conjugates with catalase and polymer peroxidase (p-peroxidase) obtained during covalent binding of enzymes with aldehyde dextrans was indirectly characterized by inhibition of adrenaline autoxidation in 0.1 M bicarbonate buffer, pH 10.2, and in microemulsion of 0.1 M aerosol OT (AOT) and Triton X-45 in octane containing 15% aqueous phase. Bicarbonates 270-281 superoxide dismutase 1 Homo sapiens 48-51 9331967-3 1997 The inhibition constants Ki for SOD and its conjugate (SOD-catalase)mic in 0.1 M bicarbonate buffer, pH 10.2, were 0.1 and 0.25 microM, respectively. Bicarbonates 81-92 superoxide dismutase 1 Homo sapiens 55-58 8036558-6 1994 The values of Als (distinguished by type of treatment of chronic renal failure) show end confirm the improvement of the situation of aluminium accumulation, specially as regards bicarbonate HD where the percentage of patients with Als > 100 micrograms/l decreases from 10.5% in 1986 to 1.7% in 1990. Bicarbonates 178-189 superoxide dismutase 1 Homo sapiens 14-17 2164216-2 1990 Using EPR and the spin traps 5,5-dimethyl-1-pyrroline 1-oxide (DMPO) and N-tert-butyl-alpha-phenylnitrone (PBN), we have shown that Cu,Zn-SOD catalyzes the formation of "free" .OH radicals from H2O2 in pH 7.6 bicarbonate buffer. Bicarbonates 209-220 superoxide dismutase 1 Homo sapiens 132-141