Abstract
Dichloromethane (CH2Cl2) is a widely used industrial solvent and a known carcinogen. Some bacterial strains are capable of metabolizing CH2Cl2 as their sole source of carbon and energy. The key enzyme in the degradation of dichloromethane by these bacteria is dichloromethane dehalogenase. This enzyme catalyzes the glutathione (GSH)–dependent dehalogenation of dichloromethane to formaldehyde and inorganic chloride. Bacterial dichloromethane dehalogenases, functionally and by their sequences, belong to class members of the glutathione S-transferase (GST) supergene family.1 In order to investigate the role and importance of different residues for substrate binding, GSH affinity, and catalytic activity of bacterial dichloromethane dehalogenases, we have initiated site-directed mutagenesis studies of the dichloromethane dehalogenase from Methylophilus sp. strain DM11.
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