Spectroscopic and potentiometric studies on the interaction of trans-[(MeH2N)2Pt(mcyt)2PdCl]NO 3(mcyt = 1-methylcytosinate) with derivatives of amino acids

I. Sóvágó, Attila Kiss, Bernhard Lippert

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The interaction of the mixed-metal complex trans-[(MeH2N)2Pt(mcyt)2PdCl]NO3 (mcyt = 1-methyl-cytosinate) with various derivatives of amino acids mimicking the side-chain metal binding sites of proteins were studied by 1H NMR, spectrophotometric and potentiometric methods. The derivatives included N-acetylamino acids (N-acetyl-methionine, -cysteine, -lysine, -histidine and -histamine), amino acids (glycine and methionine) and dipeptides (Gly-Met and Gly-Lys). The coordination of independent thioether, amino or imidazole nitrogen side-chain donor groups resulted in the formation of stable mono- or di-nuclear adducts. The formation of dinuclear complexes was characteristic of dipeptides and N-acetyl-histidine and -histamine. The existence of linkage isomers was demonstrated in the latter case, the Pd-N(3) (imidazole) isomers being more favoured. The possibility of stable chelate formation with palladium(II) (e.g. S,O for N-acetylcysteine and S, N for methionine) significantly enhanced the decomposition of the mixed-metal complex, leading to trans-[Pt(NH2Me)2(Hmcyt)2]2+.

Original languageEnglish
Pages (from-to)489-494
Number of pages6
JournalJournal of the Chemical Society, Dalton Transactions
Issue number3
DOIs
Publication statusPublished - 1995

Fingerprint

Dipeptides
Coordination Complexes
Histidine
Isomers
Methionine
Histamine
Acetylcysteine
Derivatives
Amino Acids
Palladium
Sulfides
Glycine
Lysine
Nitrogen
Metals
Binding Sites
Nuclear magnetic resonance
Decomposition
Acids
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

@article{36ccaa1bae124f4081e2dad46a5c204c,
title = "Spectroscopic and potentiometric studies on the interaction of trans-[(MeH2N)2Pt(mcyt)2PdCl]NO 3(mcyt = 1-methylcytosinate) with derivatives of amino acids",
abstract = "The interaction of the mixed-metal complex trans-[(MeH2N)2Pt(mcyt)2PdCl]NO3 (mcyt = 1-methyl-cytosinate) with various derivatives of amino acids mimicking the side-chain metal binding sites of proteins were studied by 1H NMR, spectrophotometric and potentiometric methods. The derivatives included N-acetylamino acids (N-acetyl-methionine, -cysteine, -lysine, -histidine and -histamine), amino acids (glycine and methionine) and dipeptides (Gly-Met and Gly-Lys). The coordination of independent thioether, amino or imidazole nitrogen side-chain donor groups resulted in the formation of stable mono- or di-nuclear adducts. The formation of dinuclear complexes was characteristic of dipeptides and N-acetyl-histidine and -histamine. The existence of linkage isomers was demonstrated in the latter case, the Pd-N(3) (imidazole) isomers being more favoured. The possibility of stable chelate formation with palladium(II) (e.g. S,O for N-acetylcysteine and S, N for methionine) significantly enhanced the decomposition of the mixed-metal complex, leading to trans-[Pt(NH2Me)2(Hmcyt)2]2+.",
author = "I. S{\'o}v{\'a}g{\'o} and Attila Kiss and Bernhard Lippert",
year = "1995",
doi = "10.1039/DT9950000489",
language = "English",
pages = "489--494",
journal = "Dalton Transactions",
issn = "1472-7773",
publisher = "Royal Society of Chemistry",
number = "3",

}

TY - JOUR

T1 - Spectroscopic and potentiometric studies on the interaction of trans-[(MeH2N)2Pt(mcyt)2PdCl]NO 3(mcyt = 1-methylcytosinate) with derivatives of amino acids

AU - Sóvágó, I.

AU - Kiss, Attila

AU - Lippert, Bernhard

PY - 1995

Y1 - 1995

N2 - The interaction of the mixed-metal complex trans-[(MeH2N)2Pt(mcyt)2PdCl]NO3 (mcyt = 1-methyl-cytosinate) with various derivatives of amino acids mimicking the side-chain metal binding sites of proteins were studied by 1H NMR, spectrophotometric and potentiometric methods. The derivatives included N-acetylamino acids (N-acetyl-methionine, -cysteine, -lysine, -histidine and -histamine), amino acids (glycine and methionine) and dipeptides (Gly-Met and Gly-Lys). The coordination of independent thioether, amino or imidazole nitrogen side-chain donor groups resulted in the formation of stable mono- or di-nuclear adducts. The formation of dinuclear complexes was characteristic of dipeptides and N-acetyl-histidine and -histamine. The existence of linkage isomers was demonstrated in the latter case, the Pd-N(3) (imidazole) isomers being more favoured. The possibility of stable chelate formation with palladium(II) (e.g. S,O for N-acetylcysteine and S, N for methionine) significantly enhanced the decomposition of the mixed-metal complex, leading to trans-[Pt(NH2Me)2(Hmcyt)2]2+.

AB - The interaction of the mixed-metal complex trans-[(MeH2N)2Pt(mcyt)2PdCl]NO3 (mcyt = 1-methyl-cytosinate) with various derivatives of amino acids mimicking the side-chain metal binding sites of proteins were studied by 1H NMR, spectrophotometric and potentiometric methods. The derivatives included N-acetylamino acids (N-acetyl-methionine, -cysteine, -lysine, -histidine and -histamine), amino acids (glycine and methionine) and dipeptides (Gly-Met and Gly-Lys). The coordination of independent thioether, amino or imidazole nitrogen side-chain donor groups resulted in the formation of stable mono- or di-nuclear adducts. The formation of dinuclear complexes was characteristic of dipeptides and N-acetyl-histidine and -histamine. The existence of linkage isomers was demonstrated in the latter case, the Pd-N(3) (imidazole) isomers being more favoured. The possibility of stable chelate formation with palladium(II) (e.g. S,O for N-acetylcysteine and S, N for methionine) significantly enhanced the decomposition of the mixed-metal complex, leading to trans-[Pt(NH2Me)2(Hmcyt)2]2+.

UR - http://www.scopus.com/inward/record.url?scp=37049082819&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=37049082819&partnerID=8YFLogxK

U2 - 10.1039/DT9950000489

DO - 10.1039/DT9950000489

M3 - Article

AN - SCOPUS:37049082819

SP - 489

EP - 494

JO - Dalton Transactions

JF - Dalton Transactions

SN - 1472-7773

IS - 3

ER -