Organometallic complexes with biological molecules: XII. Solid-state and solution studies on dialkyltin(IV)- and trialkyltin(IV)-thiaminepyrophosphate derivatives

Fiore, Tiziana; Pellerito, Claudia; Fontana, Alberta; Triolo, Fabio; Maggio, Francesco; Pellerito, Lorenzo; Cestelli, Alessandro; Liegro, Italia Di

doi:10.1002/(sici)1099-0739(199910)13:10<705::aid-aoc917>3.0.co;2-8

Cited by 12 publications

(12 citation statements)

References 31 publications

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“…The interactions of dibutyltin(IV)-thiaminepyrophosphate(DBTPP) and tributyltin(IV)-thiaminepyrophosphate (TBTPP) complexes with Bluescript KS plasmid and immortalized 3T3 fibroblasts were studied [185]. Both compounds have a clear inhibitory effect on the growth of immortalized mouse embryonal fibroblasts (NIH-3T3), TBTPP being much more active.…”

Section: Biological Effects Of Organotin(iv) Complexesmentioning

confidence: 93%

Biological activity studies on organotin(IV)n+ complexes and parent compounds

Pellerito

Nagy

Pellerito

et al. 2006

Journal of Organometallic Chemistry

194

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Section: Biological Effects Of Organotin(iv) Complexesmentioning

confidence: 93%

Biological activity studies on organotin(IV)n+ complexes and parent compounds

Pellerito

Nagy

Pellerito

et al. 2006

Journal of Organometallic Chemistry

194

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“…Studies have mainly addressed the formation equilibria of its complexes with metal cations, and the structures of these complexes in solution: NMR measurements and other data suggest that thiamine diphosphate binds to metal ions in solution via both the diphosphate group and also, except in a rhodium(III) complex, via the pyrimidine N(1‘) atom 5f. By contrast, very few complexes between thiamine diphosphate and metal ions have been isolated and characterized in the solid state, and in the only two that have been studied by X-ray diffractometry, 6a,d thiamine diphosphate is bound to the metal ion only via the diphosphate group. It is this latter binding mode that has been observed in all X-ray crystallographic studies of thiamine-diphosphate-dependent enzymes, and it is on the basis of these studies that it is commonly assumed that the only role of the M(II) cation in the mechanism of the enzyme is to anchor the thiamine diphosphate molecule in the active site.…”

Section: Introductionmentioning

confidence: 99%

The Reaction of Dimethyltin(IV) Dichloride with Thiamine Diphosphate (H₂TDP): Synthesis and Structure of [SnMe₂(HTDP)(H₂O)]Cl·H₂O, and Possibility of a Hitherto Unsuspected Role of the Metal Cofactor in the Mechanism of Vitamin-B₁-Dependent Enzymes

et al. 2004

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The complex [SnMe(2)(HTDP)(H(2)O)]Cl.H(2)O, synthesized by reaction between dimethyltin(IV) dichloride and thiamine diphosphate hydrochloride (H(3)TDPCl) in water, was characterized by X-ray diffractometry and IR and Raman spectroscopy in the solid state, and by electrospray mass spectrometry (ESMS) and NMR spectroscopy ((1)H, (13)C, (31)P, (119)Sn and inverse-detection (1)H,(15)N HMBC) in aqueous solution. In the solid state the HTDP(-) anion chelates the metal via one oxygen atom of each phosphate group [Sn-O = 2.062(3), 2.292(3) A], and another oxygen atom belonging to the terminal phosphate links the SnMe(2)(2+) cations into chains. The tin atom has distorted octahedral coordination involving the trans methyl groups, the above-mentioned diphosphate oxygen atoms, and the oxygen atom of the coordinated water molecule. The thiamine moiety has F conformation. NMR studies suggest that the interaction between the organometallic cation and the HTDP(-) ligand persists in D(2)O solution, which is in keeping with the ESMS spectrum showing a peak corresponding to [SnMe(2)(HTDP)]. Both in the solid state and in solution, the acidic HTDP(-) proton in the complex is located on the N(1') atom of the pyrimidine ring. The enzymatic behavior of native pyruvate decarboxylase (EC 4.1.1.1, PDC), obtained from baker's yeast, was compared in a coupled assay with that shown by the "SnMe(2)-holoenzyme" created by incubation of apoPDC with [SnMe(2)(HTDP)(H(2)O)]Cl.H(2)O. The SnMe(2)-holoenzyme exhibited about 34% of the activity of the native enzyme (with a Michaelis-Menten constant of 2.7 microM, as against 6.4 microM for native PDC), so confirming the very low specificity of PDC regarding the identity of its metal ion cofactor. In view of the observed protonation of N(1'), it is suggested that the role of divalent cations in the mechanism of thiamine-diphosphate-dependent enzymes may be not only to anchor the cofactor in its binding site but also to shift the acidic proton of HTDP(-) from the diphosphate group to N(1'); protonation of N(1') is widely believed to be important for enzyme function, but the origin of the proton has never been clarified.

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“…In the mixed complex of Cu(II) with phenanthroline and the thiamine diphosphate zwitterion, the latter chelates the metal via one oxygen of each phosphate group, creating a six-membered metallacycle, and this coordination mode is also generally observed in X-ray studies of enzymes that depend on thiamine diphosphate . IR and NMR studies of thiamine diphosphate have likewise mostly pointed to chelation via P(1)−O and P(2)−O groups (with or without additional metal bonding by the pyrimidine N(1‘) atom), ,, although the formation of complexes in which coordination via a P(1)−O group is weak 24f or even absent 24d in solution has also been suggested on the basis of 31 P NMR findings. Bidentate coordination via the terminal phosphate group in the solid state has been hypothesized for a complex of thiamine diphosphate and VO 2+ on the basis of IR data, but no confirmatory X-ray study has been carried out 24e…”

Section: Resultsmentioning

confidence: 99%

“…While this work was in progress, some methyl and butyltin(IV) complexes of H 2 TDP were prepared by Fiore et al, but the coordination mode of thiamine diphosphate in these complexes was not conclusively determined.…”

Section: Introductionmentioning

confidence: 99%

Reaction of Thiamine Diphosphate Hydrochloride (H₃TDPCl) With Methylphenyltin(IV) Dichloride in Water. Molecular and Crystal Structures of the Oxygen−Capped Cluster [{SnMe(HTDP)(OH)}₃O](OH)·21H₂O, in Which Thiamine Diphosphate Coordinates via Its Terminal Phosphate Group

et al. 2001

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Reaction between thiamine diphosphate hydrochloride (H 3 TDPCl) and methylphenyltin dichloride in water at pH ca. 5.6 afforded the title complex, which was studied by X-ray diffraction and IR and Raman spectroscopy in the solid state and by multinuclear NMR spectroscopy ( 1 H, 13 C, 31 P, and 119 Sn) in aqueous solution. The crystals of this compound are formed by the oxygen-capped cluster cation [{SnMe(HTDP)(OH)} 3 O] + , an OHcounterion, and water of crystallization. The cation has 3-fold symmetry, and the tin atom has coordination number 6 and a distorted octahedral coordination polyhedron. The HTDPanion is bis-monodentate bridging between two Sn atoms via two of the oxygens belonging to the terminal phosphate of the ethyl diphosphate side chain [Sn-O ) 2.074(3), 2.100( 5) Å]. The thiamine moiety has F conformation, with torsion angles C(2)-N(3)-C(3,5′)-C(5′) ) -5.8(11)°and N(3)-C(3,5′)-C(5')-C( 4′) ) -83.0(10)°, and the ethyl diphosphate side chain is folded back, directing the pyrimidine and thiazolium rings of the three HTDPanions away from the "missing" corner of the Sn 3 O 4 core so that they form the walls of a "nest" with the core as its floor. Although the diffraction data do not allow direct location of most of the hydrogen atoms, indirect structural evidence suggests (i) that the OHcounterion lies inside the nest on the 3-fold symmetry axis, (ii) that the remaining dissociable proton of the HTDPanion forms a strong hydrogen bond between the pyrimidine N(1′) atom and the uncoordinated oxygen of the terminal phosphate of another HTDPbelonging to the same cluster, and (iii) that one of the oxygens of the nonterminal phosphate is hydrogen-bonded to one of the -OH groups that bridge between the Sn atoms. Features ii and iii are probably responsible for the folding of the ethyl diphosphate side chain. Hydrogen bonds involving the N(4′R)-H 2 group on the pyrimidine ring and the water molecules of crystallization are also present. The multinuclear NMR results indicate that most of the structural features exhibited by the cluster in the solid state remain in D 2 O solution. IR and Raman spectra are also discussed.

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Organometallic complexes with biological molecules: XII. Solid-state and solution studies on dialkyltin(IV)- and trialkyltin(IV)-thiaminepyrophosphate derivatives

Cited by 12 publications

References 31 publications

Biological activity studies on organotin(IV)n+ complexes and parent compounds

Biological activity studies on organotin(IV)n+ complexes and parent compounds

The Reaction of Dimethyltin(IV) Dichloride with Thiamine Diphosphate (H₂TDP): Synthesis and Structure of [SnMe₂(HTDP)(H₂O)]Cl·H₂O, and Possibility of a Hitherto Unsuspected Role of the Metal Cofactor in the Mechanism of Vitamin-B₁-Dependent Enzymes

Reaction of Thiamine Diphosphate Hydrochloride (H₃TDPCl) With Methylphenyltin(IV) Dichloride in Water. Molecular and Crystal Structures of the Oxygen−Capped Cluster [{SnMe(HTDP)(OH)}₃O](OH)·21H₂O, in Which Thiamine Diphosphate Coordinates via Its Terminal Phosphate Group

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Organometallic complexes with biological molecules: XII. Solid-state and solution studies on dialkyltin(IV)- and trialkyltin(IV)-thiaminepyrophosphate derivatives

Cited by 12 publications

References 31 publications

Biological activity studies on organotin(IV)n+ complexes and parent compounds

Biological activity studies on organotin(IV)n+ complexes and parent compounds

The Reaction of Dimethyltin(IV) Dichloride with Thiamine Diphosphate (H2TDP): Synthesis and Structure of [SnMe2(HTDP)(H2O)]Cl·H2O, and Possibility of a Hitherto Unsuspected Role of the Metal Cofactor in the Mechanism of Vitamin-B1-Dependent Enzymes

Reaction of Thiamine Diphosphate Hydrochloride (H3TDPCl) With Methylphenyltin(IV) Dichloride in Water. Molecular and Crystal Structures of the Oxygen−Capped Cluster [{SnMe(HTDP)(OH)}3O](OH)·21H2O, in Which Thiamine Diphosphate Coordinates via Its Terminal Phosphate Group

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The Reaction of Dimethyltin(IV) Dichloride with Thiamine Diphosphate (H₂TDP): Synthesis and Structure of [SnMe₂(HTDP)(H₂O)]Cl·H₂O, and Possibility of a Hitherto Unsuspected Role of the Metal Cofactor in the Mechanism of Vitamin-B₁-Dependent Enzymes

Reaction of Thiamine Diphosphate Hydrochloride (H₃TDPCl) With Methylphenyltin(IV) Dichloride in Water. Molecular and Crystal Structures of the Oxygen−Capped Cluster [{SnMe(HTDP)(OH)}₃O](OH)·21H₂O, in Which Thiamine Diphosphate Coordinates via Its Terminal Phosphate Group