Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols

Xie Yuchun, Prasanta Kumar Das, Jose M.M. Caaveiro, Alexander M. Klibanov

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Lyophilized horseradish peroxidase (HRP) exhibits poor stereoselectivity in the sulfoxidation of thioanisole when the enzyme is either redissolved in water orsuspendedinorganicsolvents.However,whenHRPis 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 hypothesisis 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.
Original languageEnglish
Pages (from-to)105-111
Number of pages7
JournalBiotechnology and Bioengineering
Volume79
Issue number1
DOIs
Publication statusPublished - 2002

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Stereoselectivity
Peroxidase
Alcohols
Enzymes
Horseradish Peroxidase
Molecular Dynamics Simulation
Isomers
Organic solvents
Molecular dynamics
Catalytic Domain
Crystal structure
Ligands
X-Rays
X rays
Water
Substrates
methylphenylsulfide

Cite this

Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols. / Yuchun, Xie; Das, Prasanta Kumar; Caaveiro, Jose M.M.; Klibanov, Alexander M.

In: Biotechnology and Bioengineering, Vol. 79, No. 1, 2002, p. 105-111.

Research output: Contribution to journalArticle

Yuchun, Xie ; Das, Prasanta Kumar ; Caaveiro, Jose M.M. ; Klibanov, Alexander M. / Unexpectedly enhanced stereoselectivity of peroxidase-catalyzed sulfoxidation in branched alcohols. In: Biotechnology and Bioengineering. 2002 ; Vol. 79, No. 1. pp. 105-111.
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