Asymmetric periodate oxidation of functionalized sulfides catalyzed by bovine serum albumin

Colonna, Stefano; Banfi, Stefano; Fontana, Francesca; SOMMARUGA, M.

doi:10.1021/jo00206a008

Cited by 46 publications

(15 citation statements)

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“…Under the same experimental conditions as above, the v enz values for the formation of both enantiomers of phenyl isobutyl sulfoxide in the presence of BSA were almost six fold higher than v aq but showed no stereoselectivity (Table I). Thus, although BSA accelerated the oxidation of 1, it did so non-stereoselectively [in contrast to the previous reports (Sugimoto et al 1979(Sugimoto et al , 1981Colonna et al, 1985Colonna et al, , 1986] presumably because of the multiplicity of the hydrophobic binding sites.…”

Section: Resultscontrasting

confidence: 85%

Asymmetric sulfoxidations mediated by α‐chymotrypsin

Das

Caaveiro

Luque

et al. 2002

Biotech & Bioengineering

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The oxidation of aryl alkyl sulfides with H(2)O(2) in aqueous solution is a reasonably facile reaction producing racemic sulfoxides. We show that in the presence of the hydrolytic enzyme alpha-chymotrypsin such a sulfoxidation is accelerated and, more importantly, becomes stereoselective. With phenyl isobutyl sulfide as a model, the chymotrypsin-mediated, highly asymmetric oxidation is shown to occur in the hydrophobic binding pocket of the enzyme active site. The stereoselectivity of the chymotrypsin-mediated sulfoxidations is correctly explained by means of structure-based molecular modeling of the enzyme-sulfide complexes.

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Section: Resultscontrasting

confidence: 85%

Asymmetric sulfoxidations mediated by α‐chymotrypsin

Das

Caaveiro

Luque

et al. 2002

Biotech & Bioengineering

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“…These transport proteins have been shown to catalyze a variety of enantioselective transformations, including oxidation,29–31 reduction,32, 33 and Diels–Alder cycloaddition34 reactions, with moderate to good enantioselectivities (Scheme 2) 35…”

Section: Supramolecular Anchoring Strategiesmentioning

confidence: 99%

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

Letondor¹,

Ward²

2006

ChemBioChem

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Creating new catalytic function in proteins. Anchoring an organometallic moiety within a protein affords artificial metalloenzymes for enantioselective catalysis. Both chemical and genetic tools can be applied in the optimization of such systems, which lie at the interface between homogeneous and enzymatic catalysis. This minireview presents the latest developments in the field of artificial metalloenzymes.

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“…In this context of supramolecular anchoring of cofactors, serum albumin plays a key role; it functions as a transport protein in plasma and shows a unique ability to bind a variety of hydrophobic molecules, including steroids, fatty acids and heme. [29] In addition, serum albumins, especially the bovine one, have been shown to catalyze enantioselective transformations such as oxidations, [30,31] reductions [32] and Diels-Alder cycloadditions with moderate to good enantioselectivity. [33] We have chosen Mn-salen catalysts, which are well-known systems for selective oxidation catalysis in organic solvents, because of their broad catalytic properties.…”

Section: Resultsmentioning

confidence: 99%

The Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

et al. 2009

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MAGIC Mn-salen mETALLOZYME: The design of an original, artificial, inorganic, complex-protein adduct, has led to a better understanding of the synergistic effects of both partners. The exclusive formation of sulfoxides by the hybrid biocatalyst, as opposed to sulfone in the case of the free inorganic complex, highlights the modulating role of the inorganic-complex-binding site in the protein. Artificial metalloenzymes based on the incorporation of Mn-salen complexes into human serum albumin display high efficiency and selectivity for sulfoxide production during sulfide oxidation. The reactions carried out by the artificial metallozymes are comparable to those carried out by natural biocatalysis. We have found that the polarity of the protein environment is crucial for selectivity and that a synergy between both partners of the hybrid results in the novel activity.

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Asymmetric periodate oxidation of functionalized sulfides catalyzed by bovine serum albumin

Cited by 46 publications

References 0 publications

Asymmetric sulfoxidations mediated by α‐chymotrypsin

Asymmetric sulfoxidations mediated by α‐chymotrypsin

Artificial Metalloenzymes for Enantioselective Catalysis: Recent Advances

The Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

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