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 language | English |
|---|---|
| Pages (from-to) | 23-36 |
| Number of pages | 14 |
| Journal | Biocatalysis and Biotransformation |
| Volume | 1 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1 Jan 1987 |
Funding
The authors would like to thank Donna Balaam for technical assistance and Mr I. Kaytal for running the mass spectra. DJL is grateful to Allelix Inc., Mississauga, Ontario, Canada, for financial support.
Keywords
- Active site
- Hydroxylation selectivity
- Methylococcus capsulatus
- Monooxygenase
ASJC Scopus subject areas
- Biochemistry
- Biotechnology
- Catalysis
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