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 journalArticlepeer-review

11 Citations (Scopus)


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
Issue number1
Publication statusPublished - 2002


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