Studies on the regioselectivity and stereoselectivity of the soluble methane monooxygenase from methylococcus capsulatus (Bath)

David J. Leak, Howard Dalton

Research output: Contribution to journalArticle

Abstract

Alkyl substituted derivatives of cyclohexane and cyclohexene have been used as active site probes of the soluble methane monooxygenase (MMO) from Methylococcus capsulatus (Bath). It is proposed that the products obtained are those that would be predicted on the grounds of chemical reactivity modulated by two enzymic constraints (i) steric hindrance favouring hydroxylation at positions distal to bulky substituents and (ii) limited penetration of the substrate beyond the active site of oxygen insertion. Evidence for inversion of stereochemistry during the hydroxylation of cis-dimethylcyclohexane and rearrangement during the hydroxylation of 3-methyl-1-cyclohexene supports the suggestion that a stepwise mechanism (hydrogen abstraction and hydroxylation) operates in the hydroxylation of aliphatic carbons.

Original languageEnglish
Pages (from-to)23-36
Number of pages14
JournalBiocatalysis and Biotransformation
Volume1
Issue number1
DOIs
Publication statusPublished - 1 Jan 1987

Keywords

  • Active site
  • Hydroxylation selectivity
  • Methylococcus capsulatus
  • Monooxygenase

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Catalysis

Cite this

@article{9838a0c06bb44d418ca572b8de2da8ea,
title = "Studies on the regioselectivity and stereoselectivity of the soluble methane monooxygenase from methylococcus capsulatus (Bath)",
abstract = "Alkyl substituted derivatives of cyclohexane and cyclohexene have been used as active site probes of the soluble methane monooxygenase (MMO) from Methylococcus capsulatus (Bath). It is proposed that the products obtained are those that would be predicted on the grounds of chemical reactivity modulated by two enzymic constraints (i) steric hindrance favouring hydroxylation at positions distal to bulky substituents and (ii) limited penetration of the substrate beyond the active site of oxygen insertion. Evidence for inversion of stereochemistry during the hydroxylation of cis-dimethylcyclohexane and rearrangement during the hydroxylation of 3-methyl-1-cyclohexene supports the suggestion that a stepwise mechanism (hydrogen abstraction and hydroxylation) operates in the hydroxylation of aliphatic carbons.",
keywords = "Active site, Hydroxylation selectivity, Methylococcus capsulatus, Monooxygenase",
author = "Leak, {David J.} and Howard Dalton",
year = "1987",
month = "1",
day = "1",
doi = "10.3109/10242428709040128",
language = "English",
volume = "1",
pages = "23--36",
journal = "Biocatalysis and Biotransformation",
issn = "1024-2422",
publisher = "Informa Healthcare",
number = "1",

}

TY - JOUR

T1 - Studies on the regioselectivity and stereoselectivity of the soluble methane monooxygenase from methylococcus capsulatus (Bath)

AU - Leak, David J.

AU - Dalton, Howard

PY - 1987/1/1

Y1 - 1987/1/1

N2 - Alkyl substituted derivatives of cyclohexane and cyclohexene have been used as active site probes of the soluble methane monooxygenase (MMO) from Methylococcus capsulatus (Bath). It is proposed that the products obtained are those that would be predicted on the grounds of chemical reactivity modulated by two enzymic constraints (i) steric hindrance favouring hydroxylation at positions distal to bulky substituents and (ii) limited penetration of the substrate beyond the active site of oxygen insertion. Evidence for inversion of stereochemistry during the hydroxylation of cis-dimethylcyclohexane and rearrangement during the hydroxylation of 3-methyl-1-cyclohexene supports the suggestion that a stepwise mechanism (hydrogen abstraction and hydroxylation) operates in the hydroxylation of aliphatic carbons.

AB - Alkyl substituted derivatives of cyclohexane and cyclohexene have been used as active site probes of the soluble methane monooxygenase (MMO) from Methylococcus capsulatus (Bath). It is proposed that the products obtained are those that would be predicted on the grounds of chemical reactivity modulated by two enzymic constraints (i) steric hindrance favouring hydroxylation at positions distal to bulky substituents and (ii) limited penetration of the substrate beyond the active site of oxygen insertion. Evidence for inversion of stereochemistry during the hydroxylation of cis-dimethylcyclohexane and rearrangement during the hydroxylation of 3-methyl-1-cyclohexene supports the suggestion that a stepwise mechanism (hydrogen abstraction and hydroxylation) operates in the hydroxylation of aliphatic carbons.

KW - Active site

KW - Hydroxylation selectivity

KW - Methylococcus capsulatus

KW - Monooxygenase

UR - http://www.scopus.com/inward/record.url?scp=0001923867&partnerID=8YFLogxK

U2 - 10.3109/10242428709040128

DO - 10.3109/10242428709040128

M3 - Article

VL - 1

SP - 23

EP - 36

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

SN - 1024-2422

IS - 1

ER -