Bicarbonate Enhances the Hydroxylation, Nitration, and Peroxidation Reactions Catalyzed by Copper, Zinc Superoxide Dismutase

Zhang, Hao; Joseph, Joy; Felix, Christopher C.; Kalyanaraman, Balaraman

doi:10.1074/jbc.275.19.14038

Cited by 122 publications

(157 citation statements)

References 32 publications

Supporting

Mentioning

147

Contrasting

Unclassified

Order By: Relevance

“…Effect of GSH on the Peroxidase Activity of LPO-The oneelectron oxidation of ABTS to ABTS ϩ ⅐ catalyzed by peroxidases has been used as an index of peroxidase activity (41,46). We examined the effect of varying concentrations of GSH on the rate of ABTS oxidation catalyzed by LPO (Fig.…”

Section: Investigation Of the Involvement Of Amino Acid Residues In Tmentioning

confidence: 99%

See 1 more Smart Citation

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Guo

Detweiler

Mason

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

A novel anti-5,5-dimethyl-1-pyrroline N-oxide (DMPO) polyclonal antiserum that specifically recognizes protein radical-derived DMPO nitrone adducts has been developed. In this study, we employed this new approach, which combines the specificity of spin trapping and the sensitivity of antigen-antibody interactions, to investigate protein radical formation from lactoperoxidase (LPO). When LPO reacted with GSH in the presence of DMPO, we detected an LPO radical-derived DMPO nitrone adduct using enzyme-linked immunosorbent assay and Western blotting. The formation of this nitrone adduct depended on the concentrations of GSH, LPO, and DMPO as well as pH values, and GSH could not be replaced by H 2 O 2 . The level of this nitrone adduct was decreased significantly by azide, catalase, ascorbate, iodide, thiocyanate, phenol, or nitrite. However, its formation was unaffected by chemical modification of free cysteine, tyrosine, and tryptophan residues on LPO. ESR spectra showed that a glutathiyl radical was formed from the LPO/GSH/DMPO system, but no protein radical adduct could be detected by ESR. Its formation was decreased by azide, catalase, ascorbate, iodide, or thiocyanate, whereas phenol or nitrite increased it. GSH caused marked changes in the spectrum of compound II of LPO, indicating that GSH binds to the heme of compound II, whereas phenol or nitrite prevented these changes and reduced compound II back to the native enzyme. GSH also dose-dependently inhibited the peroxidase activity of LPO as determined by measuring 2,2 -azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) oxidation. Taken together, these results demonstrate that the GSH-dependent LPO radical formation is mediated by the glutathiyl radical, possibly via the reaction of the glutathiyl radical with the heme of compound II to form a heme-centered radical trapped by DMPO.

show abstract

Section: Investigation Of the Involvement Of Amino Acid Residues In Tmentioning

confidence: 99%

“…Effect of GSH on the Peroxidase Activity of LPO-Peroxidase activity was measured using ABTS (41,46) or guaiacol (22,47) as an electron donor. For ABTS oxidation, 0.2 M LPO was preincubated with various concentrations of GSH for 60 min in 96-well plates (Corning Inc., Corning, NY).…”

Section: Effect Of Gsh On the Spectrum Of Compound II Of Lpo In The Pmentioning

confidence: 99%

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Guo

Detweiler

Mason

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…2), suggesting that catalase addition was enough to minimize Fenton chemistry during acetaldehyde oxidation by XO. The iron-superoxide dismutase enzyme was used in these experiments, because it has not been reported to display the peroxidase activity that oxidizes the bicarbonate/carbon dioxide pair in contrast with the Cu,Znsuperoxide dismutase enzyme (22)(23)(24)(25)(26)(27).…”

Section: Production Of Radicals Monitored By Dhr Oxidation-dhrmentioning

confidence: 99%

“…In addition to being considered an important mediator of peroxynitrite effects in vivo (reviewed in Refs. 20 and 21), the carbonate radical anion has been proposed as the diffusible oxidant produced during the peroxidase activity of the enzyme Cu,Zn-superoxide dismutase (22)(23)(24)(25)(26)(27), whose relationship to the familial amyothophic lateral sclerosis disease remains under scrutiny.…”

mentioning

confidence: 99%

Production of the Carbonate Radical Anion during Xanthine Oxidase Turnover in the Presence of Bicarbonate

Bonini¹,

Miyamoto²,

Mascio

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Xanthine oxidase is generally recognized as a key enzyme in purine catabolism, but its structural complexity, low substrate specificity, and specialized tissue distribution suggest other functions that remain to be fully identified. The potential of xanthine oxidase to generate superoxide radical anion, hydrogen peroxide, and peroxynitrite has been extensively explored in pathophysiological contexts. Here we demonstrate that xanthine oxidase turnover at physiological pH produces a strong one-electron oxidant, the carbonate radical anion. The radical was shown to be produced from acetaldehyde oxidation by xanthine oxidase in the presence of catalase and bicarbonate on the basis of several lines of evidence such as oxidation of both dihydrorhodamine 123 and 5,5-dimethyl-1-pyrroline-N-oxide and chemiluminescence and isotope labeling/mass spectrometry studies. In the case of xanthine oxidase acting upon xanthine and hypoxanthine as substrates, carbonate radical anion production was also evidenced by the oxidation of 5,5-dimethyl-1-pyrroline-N-oxide and of dihydrorhodamine 123 in the presence of uricase. The results indicated that Fenton chemistry occurring in the bulk solution is not necessary for carbonate radical anion production. Under the conditions employed, the radical was likely to be produced at the enzyme active site by reduction of a peroxymonocarbonate intermediate whose formation and reduction is facilitated by the many xanthine oxidase redox centers. In addition to indicating that the carbonate radical anion may be an important mediator of the pathophysiological effects of xanthine oxidase, the results emphasize the potential of the bicarbonate-carbon dioxide pair as a source of biological oxidants.

show abstract

“…Any valid mechanism must explain the dual requirement for HCO 3 Ϫ and CO 2 and also the involvement of O 2 Ϫ . Moreover, analogy with the Cu,ZnSOD ϩ H 2 O 2 system indicates that CO 3 •Ϫ is a likely participant, whereas HO • is not (1,(3)(4)(5)(6)(7)(8) Ϫ , yet rapid H 2 O 2 consumption is a hallmark of this process.…”

mentioning

confidence: 99%

Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions

Liochev

Fridovich²

2004

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Mn(II) can catalyze the decomposition of H2O2 and, in the presence of H 2O2, can catalyze the oxidation of NADH. Strikingly, these processes depend on the simultaneous presence of both CO 2 and HCO 3 ؊ . This explains the exponential dependence of the rates on Materials and MethodsNaHCO 3 , MnCl 2 , sodium pyrophosphate, and H 2 O 2 were from Mallinckrodt; Tris was from Merck; catalase was from Roche Molecular Biochemicals; human MnSOD was from Biotechnology General (Rehovot, Israel); and NADH was from Sigma. Reaction mixtures usually contained 10 mM H 2 O 2 , 0.1 mM MnCl 2 , and 20 mM NaHCO 3 in 100 mM Tris buffer at pH 7.4 and room temperature (23°C). Reactions were followed spectrophotometrically, and in cases where the addition of reactants entailed sudden changes in absorbance, due either to dilution or the absorbance of the reagent added, such changes were corrected in the data shown. When absorbance changes with time were too rapid to record, they are shown as dashed lines as in Fig. 3. CO 2 was added as ice-cold water saturated with CO 2 gas. ResultsAbsorption Spectra. Addition of the third component (H 2 O 2 or MnCl 2 , or NaHCO 3 ), to Tris-buffered solutions of the other two, initiated the changes in absorption spectrum shown in Fig. 1. It should be noted that several buffering species were explored, including phosphate, cacodylate, and Hepes, but only Tris supported the changes observed. Fig. 1 A shows that the most rapid (0 -3 min) was an increase in absorbance in the range of 250 -350 nm and a decrease at wavelengths Ͻ250 nm. At longer reaction times (0 -20 min), absorbance appeared at Ϸ270 nm, whereas the absorbance Ͻ250 nm first decreased and then increased, as shown in Fig. 1B. At still longer times (Fig. 1C), the band at Ϸ270 nm became more pronounced, a shoulder developed at Ϸ300 nm, and absorbance Ͻ250 nm decreased.The species responsible for the absorbance centered at 270 nm is some stable product of Tris oxidation, as similar absorbance is seen in Tris buffer that has aged for many months. The kinetics of the absorbance change at 270 nm is shown in Fig. 2. Starting the reaction by adding NaHCO 3 caused a small but rapid increase at 270 nm, which was followed by a slower increase that was not interrupted by late addition of 48 g͞ml MnSOD, 0.5 mM pyrophosphate, or 120 units͞ml catalase, any of which inhibited if present at the outset. The initial rapid increase at 270 nm was due to the rapidly formed species absorbing in the 250-to 350-nm region. Evidently, the stable A 270 species is produced from a preformed precursor and does not depend on the continued presence of H 2 O 2 , O 2 Ϫ , or Mn(III). The latter deduction is based on the abilities of catalase to remove H 2 O 2 , MnSOD to remove O 2 Ϫ , and pyrophosphate to complex and thus trap Mn(III).The time course of the broad band followed at Ϸ300 nm is illustrated in Fig. 3. Addition of NaHCO 3 to the buffered solution of Mn(II) ϩ H 2 O 2 caused a rapid increase in absorbance that approached a plateau. This plateau evidently represented a...

show abstract

Bicarbonate Enhances the Hydroxylation, Nitration, and Peroxidation Reactions Catalyzed by Copper, Zinc Superoxide Dismutase

Cited by 122 publications

References 32 publications

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Production of the Carbonate Radical Anion during Xanthine Oxidase Turnover in the Presence of Bicarbonate

Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions

Contact Info

Product

Resources

About