Crystal structure and spectroscopic properties of violet glutathione-copper(II) complex with axial sulfur coordination and two copper sites via a disulfide bridge

Miyoshi, Kiyonori; Sugiura, Yukio; Ishizu, Kazuhiko; Iitaka, Yōichi; Nakamura, Hakobu

doi:10.1021/ja00539a027

Cited by 81 publications

(35 citation statements)

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“…The subsequent crystallization of a Cu-GSH complex at alkaline pH indeed revealed a binuclear structure, but the ESR spectrum was different from those previously reported and did not show any sign of relaxation broadening (Miyoshi et al 1980).…”

Section: The Question Of the Second Binding Sitecontrasting

confidence: 88%

“…This is probably due to fact that alkaline pH is required to achieve crystallization; some groups have mentioned ongoing attempts to crystallize Cu(II?GSSG at neutral pH (Miyoshi et al 1980, Postal et al 1985, but no report of the successful preparation of such a crystal has appeared in the literature so far.…”

Section: Resultsmentioning

confidence: 99%

“…Crystals of a similar complex, but with a completely different ESR spectrum, were isolated by Miyoshi et al (1980); the (" 1996 Rapid Science Publishers BioMetals Vol 9 1996 3 X-ray crystallography revealed a slightly different square pyramidal Cu(1I) site, with the near sulphur acting as the axial ligand and without any bonding to the glycine carboxylate. This structure was suggested to exist also at physiological pH, on the basis of spectroscopic evidence and model studies (Miyoshi et al 1983a,b).…”

Section: Introductionmentioning

confidence: 99%

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Copper-glutathione complexes under physiological conditions: structures in solution different from the solid state coordination

Steinkühler

Weser

et al. 1996

Biometals

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The physiologically important copper complexes of oxidized glutathione have been examined by electron spin resonance (ESR) spectroscopy in aqueous solution at neutral pH. Low temperature measurements show that the Cu(ll) binding site in oxidized glutathione has the same ligand arrangement as in the copper complexes of S-methylglutathione, glutamine, glutamate and glycine. The site is composed of the amino nitrogens and the carboxyl oxygens of two ?-glutamyl residues; there is no interaction with amide nitrogens, the sulphur bond or the glycyl carboxyl groups. At high metal to ligand ratios a binuclear species exists, in which each Cu(II) binds only to one 7-glutamyl residue. The previously reported forbidden transition detected at g = 4 is due to non-specific aggregation and not to spin coupling of intramolecular sites. Liquid solution ESR spectra show the Cu(II)-glutathione complex has a lower mobility than the corresponding Cu(II)-S-methylglutathione species. From the degree of spectral anisotropy the complex with glutathione is calculated to exist as a dimer. These results demonstrate that the physiologically relevant complex between copper and oxidized glutathione in solution is completely different from the known solid state structure determined by crystallography.

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Section: The Question Of the Second Binding Sitecontrasting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Copper-glutathione complexes under physiological conditions: structures in solution different from the solid state coordination

Steinkühler

Weser

et al. 1996

Biometals

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“…The kinetics of formation, as well as the structure of copperthiol complexes, particularly those with GSH or cysteine, are well described in the literature: Cu 2ϩ is chelated by the thiolate sulfur of glutathione probably forming a 2:1 Cu 2ϩ -GSSG complex (38,39); both the complex-formation and the involved redox reaction (see Scheme 3,taken This model provides also a simple explanation for the totally different reactivities of the "small" glutathione and the "large" BSA or Hb with Cu 2ϩ and NO. The addition of GSH to the electrode chamber containing NO and Cu 2ϩ was not followed by disappearance of NO, while the incubation of GSH with Cu 2ϩ in a spectroscopic cuvette led to complete disappearance of thiols (Fig.…”

mentioning

confidence: 99%

Mechanism of S-Nitrosothiol Formation and Degradation Mediated by Copper Ions

Stubauer¹,

Giuffrè

Sarti

1999

Journal of Biological Chemistry

141

100

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Experimental evidence is presented supporting a mechanism of S-nitrosothiol formation and degradation mediated by copper ions using bovine serum albumin, human hemoglobin and glutathione as models. We found that Cu 2؉ , but not Fe 3؉ , induces in the presence of NO a fast S-nitrosation of bovine serum albumin and human hemoglobin, and the reaction is prevented by thiol blocking reagents. During the reaction, Cu ؉ is accumulated and accounts for destabilization of the S-nitrosothiol formed. In contrast, glutathione rapidly dimerizes in the presence of Cu 2؉ , the reaction competing with S-nitrosation and therefore preventing the formation of S-nitrosoglutathione. We have combined the presented role of Cu 2؉ in S-nitrosothiol formation with the known destabilizing effect of Cu ؉ , providing a unique simple picture where the redox state of copper determines either the NO release from S-nitrosothiols or the NO scavenging by thiol groups. The reactions described are fast, efficient, and may occur at micromolar concentration of all reactants. We propose that the mechanism presented may provide a general method for in vitro S-nitrosation. S-Nitrosothiols (RS-NOs)1 have a variety of biological activities, which are mostly attributed to their ability to release NO (1-3). RS-NOs are not only synthesized and administered clinically (2) but are also produced endogenously. Stamler et al. (4) reported that human plasma contains ϳ7 M RS-NOs, mostly as S-nitroso-albumin, a level unexpectedly high as the basal cellular NO level is in the low nanomolar range (5, 6). Thus, RS-NOs are considered as NO pools buffering the level of NO, which may be targeted at different sites (7). RS-NOs are also reported to be involved in the trans-S-nitrosation of proteins by transferring the NO ϩ moiety (8, 9), a process suggested to be a reversible post-translational modification regulating the activity of enzymes and receptors (3, 10, 11). (21), respectively. It is worth noticing that the reaction with water efficiently competes with direct thiol nitrosation by N 2 O 3 , due to the large molar excess of water over thiols. NAD ϩ substituting oxygen for the electron acceptor can also accelerate the reaction of NO with thiols (22). Several authors also suggested that S-nitrosation of thiols occurs by reaction with nitrosonium ions (NO ϩ ) formed either via metalcatalyzed oxidation of NO or via dinitrosyl-iron-cysteine complexes (8,21,23,24); efficiency and physiological relevance of these reactions remain unclear.In this study we have examined by spectroscopic and amperometric techniques the interaction of NO and thiols in the presence of cupric and ferric ions. Experiments have been carried out using the small tripeptide GSH (low millimolar amounts in the cell), bovine serum albumin (BSA, which is the most abundant plasma protein), and human hemoglobin (Hb). BSA and GSH both bear only one reduced cysteine per molecule (Cys-34 in BSA; Refs. 25 and 26), but, as shown below, they display in the presence of Cu 2ϩ a very different reactivity with NO...

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“…I1 apparak donc que la liaison Cu-S(1) n'engendre pas de fortes contraintes, ce qui pourrait s'expliquer par la flexibilit~ de la molecule de ligand. Par ailleurs, la valeur de l'angle de torsion de 113,1 (7) ° autour de la liaison S-S est voisine de celle observ+e 108,5 °dans le compos+ [CuII(gssg)CuIIlNa4.6H20 off gssg repr~sente le glutathion oxyd~ (Miyoshi et al, 1980). La (Fig.…”

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Un complexe dinucléaire du cuivre(II) à structure en feuillets: le catena-poly{μ-[tétrakis(carboxyméthyl)-N,N,N',N' cystaminato(4-)]-bis[aquacuivre(II)] tétrahydraté}

Dung¹,

Viossat²,

Busnot³

et al. 1985

Acta Crystallogr C

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Abstract. {[Cu2(C,2H~6N2OsS2)(H20)2].4H20}n,~=2.241mm -~, F(000)= 632, T= 294 K, final R = 0.036 for 1019 independent observed reflections. One N and two O atoms [from the same bis(carboxymethyl)amino moiety] and one O atom (from one water molecule) approximately define for each Cu the square base of a distorted octahedral environment which is achieved by longer trans axial bonds to one S atom (from a disulfide group) and to one O atom (from an adjacent ligand). Each ligand molecule chelates two Cu atoms and is also bonded via a bidendate carboxylate group to two others, thus forming layers linked to each other by water in a hydrogen-bonded network.

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Crystal structure and spectroscopic properties of violet glutathione-copper(II) complex with axial sulfur coordination and two copper sites via a disulfide bridge

Cited by 81 publications

References 0 publications

Copper-glutathione complexes under physiological conditions: structures in solution different from the solid state coordination

Copper-glutathione complexes under physiological conditions: structures in solution different from the solid state coordination

Mechanism of S-Nitrosothiol Formation and Degradation Mediated by Copper Ions

Un complexe dinucléaire du cuivre(II) à structure en feuillets: le catena-poly{μ-[tétrakis(carboxyméthyl)-N,N,N',N' cystaminato(4-)]-bis[aquacuivre(II)] tétrahydraté}

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