Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols

Xie, Yuchun ; Das, Prasanta Kumar ; Caaveiro, Jose M. M. ; Klibanov, Alexander M. (2002) Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols Biotechnology and Bioengineering, 79 (1). pp. 105-111. ISSN 0006-3592

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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/bit.103...

Related URL: http://dx.doi.org/10.1002/bit.10308

Abstract

Lyophilized horseradish peroxidase (HRP) exhibits poor stereoselectivity in the sulfoxidation of thioanisole when the enzyme is either redissolved in water or suspended in organic solvents. However, when HRP is co-lyophilized in the presence of lyoprotectants or ligands, its stereoselectivity, although still low in most organic solvents, increases up to 4-fold if assayed in secondary or tertiary alcohols (but not in their linear isomers). A mechanistic hypothesis is presented explaining this puzzling phenomenon on the basis of a model of the active site of the enzyme-substrate complex derived from its X-ray crystal structure by means of molecular dynamics and energy minimization.

Item Type:Article
Source:Copyright of this article belongs to John Wiley & Sons, Inc.
Keywords:Peroxidase; Stereoselectivity; Sulfoxidation; Lyophilization; Lyoprotectants; Excipients
ID Code:108776
Deposited On:01 Feb 2018 11:24
Last Modified:01 Feb 2018 11:24

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