Nucleophilic Displacement Reactions at the Thiolester Bond. III.<sup>1</sup> Kinetic Demonstration of Metastable Intermediates in the Hydroxylaminolysis and Methoxylaminolysis of Thiolesters and Thiolactones in Aqueous Solutions

Bruice, Thomas C.; Fedor, Leo R.

doi:10.1021/ja01076a032

Cited by 31 publications

(13 citation statements)

References 2 publications

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“…(3.93 X 10-2) (1.48 X 10" -) Glycinamide 2 69 X 10-"5 5.13 X 10-•3 8.45 X 10--5 1.14 X io-2 1 .68 X 10"2 1. 19 (1. 63 X 10-4) (1.61 X io-4) (5.06 X 10--4) Ethylenediamine • HC1…”

Section: Resultsmentioning

confidence: 99%

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Bruice¹,

Bruice²

1974

J. Am. Chem. Soc.

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“…(3.93 X 10-2) (1.48 X 10" -) Glycinamide 2 69 X 10-"5 5.13 X 10-•3 8.45 X 10--5 1.14 X io-2 1 .68 X 10"2 1. 19 (1. 63 X 10-4) (1.61 X io-4) (5.06 X 10--4) Ethylenediamine • HC1…”

Section: Resultsmentioning

confidence: 99%

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Bruice¹,

Bruice²

1974

J. Am. Chem. Soc.

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“…In order to account for the extreme sensitivity of C3 to methylamine, we suggest that there exist on C3, in the vicinity of the thioester, one or more catalytic groups that cause the elevated rate of reaction. The kinetics of the inactivation of CS by hydroxylamine differs from that of the hydroxylaminolysis of thioesters in aqueous solutions: whereas the inactivation of C3 is first order with hydroxylamine, that of the hydroxylaminolysis of thioesters contains a second-order dependence term, with the second molecule of hydroxylamine playing a catalytic role (27). The observed first-order kinetics of the hydroxylamine inactivation of C3, therefore, also leads one to predict the presence of hydroxylamine-like catalytic group(s) in the vicinity of the thioester.…”

Section: Discussionmentioning

confidence: 98%

Covalent binding and hemolytic activity of complement proteins.

Law¹,

Lichtenberg²,

Levine³

1980

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

166

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We report the inactivation of the third component of complement (C3) In this study, we treated C3 with primary amines and compared the rate of decay of C3 hemolytic activity with the rate of loss of surface-binding activity. We find both rates to be identical, indicating that both activities are causally related. We also present data to support our hypothesis (7) that there is an internal ester bond within C3 and that C3b binds to RS by the transfer of the acyl group of the internal ester to a hydroxyl group on the RS. C4 and C5 were also treated with hydroxylamine and methylamine. C4, which binds covalently to membrane surfaces (8), behaves like C3 in these experiments. C5, which does not bind covalently to cell surfaces (8), is not inactivated by hydroxylamine and methylamine.

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“…The working hypothesis from these results is that the stepwise mechanism is operating as proposed for other thioesters and that formation of the tetrahedral intermediate is rate-determining (Scheme 10). It should be noted that acyl-activated thioesters, like trifluorothioacetate, show a decreasing rate of hydrolysis as a function of increasing hydronium ion concentration below pH 2 [42,43]. These types of thioesters are not the subject of this review.…”

Section: The Acid-catalyzed Hydrolysis Of Ftcmentioning

confidence: 98%

“…Bruice and others utilized kinetics and solvent hydrogen KIEs to investigate non-enzymatic thioester hydrolysis in acidic, neutral and basic conditions [42][43][44][45]. In each case the results of these experiments pointed to a stepwise mechanism with the formation of tetrahedral intermediates.…”

Section: Thioesters: the Alkaline Hydrolysis Of Formylthiocholine (Ftc)mentioning

confidence: 99%

Mechanistic investigations of the hydrolysis of amides, oxoesters and thioesters via kinetic isotope effects and positional isotope exchange

Robins

Fogle

Marlier

2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The hydrolysis of amides, oxoesters and thioesters is an important reaction in both organic chemistry and biochemistry. Kinetic isotope effects (KIEs) are one of the most important physical organic methods for determining the most likely transition state structure and rate-determining step of these reaction mechanisms. This method induces a very small change in reaction rates, which, in turn, results in a minimum disturbance of the natural mechanism. KIE studies were carried out on both the non-enzymatic and the enzyme-catalyzed reactions in an effort to compare both types of mechanisms. In these studies the amides and esters of formic acid were chosen because this molecular structure allowed development of methodology to determine heavy-atom solvent (nucleophile) KIEs. This type of isotope effect is difficult to measure, but is rich in mechanistic information. Results of these investigations point to transition states with varying degrees of tetrahedral character that fit a classical stepwise mechanism. This article is part of a special issue entitled: Enzyme Transition States from Theory and Experiment.

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Nucleophilic Displacement Reactions at the Thiolester Bond. III.¹ Kinetic Demonstration of Metastable Intermediates in the Hydroxylaminolysis and Methoxylaminolysis of Thiolesters and Thiolactones in Aqueous Solutions

Cited by 31 publications

References 2 publications

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Covalent binding and hemolytic activity of complement proteins.

Mechanistic investigations of the hydrolysis of amides, oxoesters and thioesters via kinetic isotope effects and positional isotope exchange

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Nucleophilic Displacement Reactions at the Thiolester Bond. III.1 Kinetic Demonstration of Metastable Intermediates in the Hydroxylaminolysis and Methoxylaminolysis of Thiolesters and Thiolactones in Aqueous Solutions

Cited by 31 publications

References 2 publications

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Aminolysis of substituted phenyl quinoline-8- and -6-carboxylates with primary and secondary amines. Involvement of proton-slide catalysis

Covalent binding and hemolytic activity of complement proteins.

Mechanistic investigations of the hydrolysis of amides, oxoesters and thioesters via kinetic isotope effects and positional isotope exchange

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Product

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Nucleophilic Displacement Reactions at the Thiolester Bond. III.¹ Kinetic Demonstration of Metastable Intermediates in the Hydroxylaminolysis and Methoxylaminolysis of Thiolesters and Thiolactones in Aqueous Solutions