Novel Dehalogenase Mechanism for 2,3-dichloro-1-propanol Utilization in Pseudomonas Putida Strain MC4

Overview

Journal Appl Environ Microbiol

Specialties Environmental Health
Microbiology

Date 2012 Jul 4

PMID 22752160

Citations 3

Authors

Muhammad Irfan Arif

Ghufrana Samin

Jan G E van Leeuwen

Jantien Oppentocht

Dick B Janssen

Affiliations

Soon will be listed here.

Abstract

A Pseudomonas putida strain (MC4) that can utilize 2,3-dichloro-1-propanol (DCP) and several aliphatic haloacids and haloalcohols as sole carbon and energy source for growth was isolated from contaminated soil. Degradation of DCP was found to start with oxidation and concomitant dehalogenation catalyzed by a 72-kDa monomeric protein (DppA) that was isolated from cell lysate. The dppA gene was cloned from a cosmid library and appeared to encode a protein equipped with a signal peptide and that possessed high similarity to quinohemoprotein alcohol dehydrogenases (ADHs), particularly ADH IIB and ADH IIG from Pseudomonas putida HK. This novel dehalogenating dehydrogenase has a broad substrate range, encompassing a number of nonhalogenated alcohols and haloalcohols. With DCP, DppA exhibited a k(cat) of 17 s(-1). (1)H nuclear magnetic resonance experiments indicated that DCP oxidation by DppA in the presence of 2,6-dichlorophenolindophenol (DCPIP) and potassium ferricyanide [K(3)Fe(CN)(6)] yielded 2-chloroacrolein, which was oxidized to 2-chloroacrylic acid.

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