Haloacetonitriles Are Low KI Inhibitors of Bacterial Dichloromethane Dehalogenases

Michael S.P. Logan; Frank A. Blocki; Kurt J. Stimpfl; Lawrence P. Wackett

doi:10.1006/bbrc.1993.2557

Haloacetonitriles Are Low K_I Inhibitors of Bacterial Dichloromethane Dehalogenases

Michael S.P. Logan, Frank A. Blocki, Kurt J. Stimpfl, Lawrence P. Wackett

Synthetic Biology and Biotechnology Division

Research output: Contribution to journal › Article › peer-review

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Abstract

Distinct dichloromethane dehalogenases from Methylobacterium sp. strain DM4 and Methylophilus DM11 were inhibited by low concentrations of haloacetonitriles. Chloroacetonitrile (ClCH₂CN) showed maximal inhibition at a stoichiometry of 1 mol inhibitor: 1 mol holoenzyme for both enzymes. This stoichiometry is suggestive of one active site per holoenzyme or extreme negative cooperativity amongst the subunits. Radiolahcllcd ClCH₂CN dissociated completely or partially from the two dehalogenases, respectively, during chromatography. This suggested ClCH₂CN was bound non-covalently.

Original language	English (US)
Pages (from-to)	853-858
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	197
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1993.2557
State	Published - 1993

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title = "Haloacetonitriles Are Low KI Inhibitors of Bacterial Dichloromethane Dehalogenases",

abstract = "Distinct dichloromethane dehalogenases from Methylobacterium sp. strain DM4 and Methylophilus DM11 were inhibited by low concentrations of haloacetonitriles. Chloroacetonitrile (ClCH2CN) showed maximal inhibition at a stoichiometry of 1 mol inhibitor: 1 mol holoenzyme for both enzymes. This stoichiometry is suggestive of one active site per holoenzyme or extreme negative cooperativity amongst the subunits. Radiolahcllcd ClCH2CN dissociated completely or partially from the two dehalogenases, respectively, during chromatography. This suggested ClCH2CN was bound non-covalently.",

author = "Logan, {Michael S.P.} and Blocki, {Frank A.} and Stimpfl, {Kurt J.} and Wackett, {Lawrence P.}",

year = "1993",

doi = "10.1006/bbrc.1993.2557",

language = "English (US)",

volume = "197",

pages = "853--858",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Haloacetonitriles Are Low KI Inhibitors of Bacterial Dichloromethane Dehalogenases

AU - Logan, Michael S.P.

AU - Blocki, Frank A.

AU - Stimpfl, Kurt J.

AU - Wackett, Lawrence P.

PY - 1993

Y1 - 1993

N2 - Distinct dichloromethane dehalogenases from Methylobacterium sp. strain DM4 and Methylophilus DM11 were inhibited by low concentrations of haloacetonitriles. Chloroacetonitrile (ClCH2CN) showed maximal inhibition at a stoichiometry of 1 mol inhibitor: 1 mol holoenzyme for both enzymes. This stoichiometry is suggestive of one active site per holoenzyme or extreme negative cooperativity amongst the subunits. Radiolahcllcd ClCH2CN dissociated completely or partially from the two dehalogenases, respectively, during chromatography. This suggested ClCH2CN was bound non-covalently.

AB - Distinct dichloromethane dehalogenases from Methylobacterium sp. strain DM4 and Methylophilus DM11 were inhibited by low concentrations of haloacetonitriles. Chloroacetonitrile (ClCH2CN) showed maximal inhibition at a stoichiometry of 1 mol inhibitor: 1 mol holoenzyme for both enzymes. This stoichiometry is suggestive of one active site per holoenzyme or extreme negative cooperativity amongst the subunits. Radiolahcllcd ClCH2CN dissociated completely or partially from the two dehalogenases, respectively, during chromatography. This suggested ClCH2CN was bound non-covalently.

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SN - 0006-291X

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

Haloacetonitriles Are Low K_I Inhibitors of Bacterial Dichloromethane Dehalogenases

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