Inhibition by thiols of copper(II)-induced oxidation of oxyhemoglobin

Smith, Robert C.; Reed, Villel D.

doi:10.1016/0009-2797(92)90111-w

Cited by 14 publications

(10 citation statements)

References 17 publications

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“…We subsequently evaluated a procedure involving Cu(II)-catalyzed oxidation of thiols to disulfides, which proved to be successful. Although an uncommon method in protein purification, the Cu(II)-catalyzed oxidation of thiols to form intra- and intermolecular disulfides in proteins has been reported for bovine oxyhemoglobin, 28,29 human S100A8, 30 and bovine S100B. 23 Initial analytical-scale trials revealed that addition of Cu(II) to S100A7 under aerobic conditions resulted in nearly quantitative conversion to S100A7 ox .…”

Section: Resultsmentioning

confidence: 99%

Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)

et al. 2017

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Human S100A7 (psoriasin) is a metal-chelating protein expressed by epithelial cells. It is a 22-kDa homodimer with two EF-hand domains per subunit, and two transition-metal-binding His3Asp sites at the dimer interface. Each subunit contains two cysteine residues that can exist as free thiols (S100A7red) or as an intramolecular disulfide bond (S100A7ox). Herein, we examine the disulfide bond redox behavior, the Zn(II) binding properties, and the antibacterial activity of S100A7, as well as the effect of Ca(II) ions on these properties. In agreement with prior work, (Hein et al. Proc. Natl. Acad. Sci. U. S. A. 2013, 112, 13039–13044), we show that apo S100A7ox is a substrate for the mammalian thioredoxin system; however, negligible reduction of the disulfide bond is observed for Ca(II)- and Zn(II)-bound S100A7ox. Furthermore, metal binding depresses the midpoint potential of the disulfide bond. S100A7ox and S100A7red each coordinate two equivalents of Zn(II) with sub-nanomolar affinity in the absence and presence of Ca(II) ions, and the cysteine thiolates in S100A7red do not form a third high-affinity Zn(II) site. These results refute a prior model implicating the Cys thiolates of S100A7red in high-affinity Zn(II) binding (Hein et al. Proc. Natl. Acad. Sci. U. S. A. 2013, 112, 13039–13044). S100A7ox and the disulfide-null variants show comparable Zn(II)-depletion profiles; however, only S100A7ox exhibits antibacterial activity against several bacterial species. Metal substitution experiments suggest that the disulfide bonds in S100A7 may enhance metal sequestration by the His3Asp sites and thereby confer growth inhibitory properties to S100A7ox.

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Section: Resultsmentioning

confidence: 99%

Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)

et al. 2017

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“…Since its discovery at the turn of the century, attempts to define a physiological function of LER have been unsuccessful, especially from when Sigma Company no longer produce it. However, different physiological function for LER or its metabolites had been suggested in the literatures which include transport of cations or carbon dioxide, catalysis of carboxylation or decarboxylation reactions, mediation of thyroid or anticholinergic action (Brummel, 1985), protect oxyhemoglobin from oxidation (Smith and Reed, 1992) and scavenger of hydroxyl radicals or an inhibitor of their formation, and perhaps of singlet oxygen (Han, 1992).…”

Section: Resultsmentioning

confidence: 99%

L-ergothioneine level in red blood cells of healthy human males in the Western province of Saudi Arabia

Kumosani

2001

Exp Mol Med

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Ergothioneine is widely distributed in biological systems, particularly in red blood cells of animals. However, it's functional role in human body is not well understood. In order to investigate the biochemical effect of L-ergothioneine, its concentration changes in human blood with respect to ages in healthy individuals was first investigated. L-ergothioneine concentrations in the blood of Saudi males from western province at different stages of life were measured by the procedure of Carlsson et al., 1974. At early stages of life (1-10 years), the concentrations of LER is 1.5-2.0 mg/100 ml. It increases gradually at the age of 11-18 years where it reaches the maximum value of 3.7 mg/100 ml. Then, it declines gradually to 3.0-2.3 mg/ 100 ml during the period of 19-50 years. An increase in the level of LER (2.8 mg/100 ml) was seen at the age of 51 + .

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“…However, a copper-thiol complex could also play a role in strand scission, since MPA is known to coordinate to copper ions and [Cu(OP) 2 ] 2+ [29,30]. However, a copper-thiol complex could also play a role in strand scission, since MPA is known to coordinate to copper ions and [Cu(OP) 2 ] 2+ [29,30].…”

Section: Effect Of Varying Reductantsmentioning

confidence: 99%

Oxidative strand scission of nucleic acids by a multinuclear copper(II) complex

et al. 2002

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The compound [Cu(2)(II)(D(1))(H(2)O)(2)](ClO(4))(4).2H(2)O [D(1)=binucleating ligand with tris(2-pyridylmethyl)amine (TMPA) moieties linked in the 5-pyridyl position by a -CH(2)CH(2)- bridge] mediated efficient oxidative cleavage of pBR322 plasmid DNA under reducing conditions. A mononuclear analogue, [Cu(TMPA)(H(2)O)](ClO(4))(2), was less effective at linearizing supercoiled (Form I) plasmid DNA as compared to the binuclear complex. A new method for quenching the copper-dependent reactions has been developed to avoid plasmid scission by the binuclear complex and the standard gel loading buffer. EDTA was not sufficient for retarding copper reaction, but diethyldithiocarbamic acid was capable of inhibiting all reactivity. Investigation of oxidative cleavage of double-helical oligonucleotides by [Cu(2)(II)(D(1))(H(2)O)(2)](ClO(4))(4) confirmed the enhanced reactivity of the binuclear over the mononuclear complex and provided mechanistic insights into the nature of the reaction. Cleavage of DNA required both the binuclear complex and a reductant and likely proceeded through an O(2)-derived intermediate that does not include a diffusible hydroxyl radical. The greater efficiency of the binuclear complex relative to the mononuclear analogue is consistent with their relative abilities to activate dioxygen.

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Inhibition by thiols of copper(II)-induced oxidation of oxyhemoglobin

Cited by 14 publications

References 17 publications

Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)

Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)

L-ergothioneine level in red blood cells of healthy human males in the Western province of Saudi Arabia

Oxidative strand scission of nucleic acids by a multinuclear copper(II) complex

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