Degradation of 3-chlorobenzoate by thermophilic micro-organisms.

Thermophilic (75 degrees C), anaerobic biodegradation of chlorobenzoates was investigated using different inocula from geothermal and non-geothermal environments. Microbial dehalogenation of 3-chlorobenzoate (0.5 mmol l-1 was achieved by two mixed cultures growing anaerobically at 75 degrees C. One culture consisted of a facultative anaerobe and two obligate anaerobes, one of which was a methanogen, isolated from terrestrial sediments from hot springs in New Zealand. The other culture, derived from a non-geothermal environment, consisted of a Clostridium spp. and a non-spore-forming obligate anaerobe. No degradation of either 2-chlorobenzoate or 4-chlorobenzoate was achieved by these thermophilic cultures over the same time period. This is the first reported biotransformation of this chlorinated aromatic at a temperature of 75 degrees C.

Dehalogenation of lindane by a variety of porphyrins and corrins.

The dehalogenation of lindane by a range of hemoproteins, porphyrins, and corrins has been tested under reducing conditions in the presence of dithiothreitol. In addition, a series of porphyrin-metal ion complexes have been prepared and have also been screened for the capacity to dehalogenate lindane. Hemoglobin, hemin, hematin, and chlorophyll alpha all catalyzed the dehalogenation of lindane, as did all of the corrins tested. The porphyrins which did not contain metal centers--coproporphyrin, hematoporphyrin, protoporphyrin, and uroporphyrin--were inactive. However, when these porphyrins were then complexed with Co, Fe, Mg, Mo, Ni, or V, lindane dehalogenation was observed. In all cases, the reaction proceeded by an initial dechlorination to produce tetrachlorocyclohexene, which was further dehalogenated to yield chlorobenzene as the end product.

Degradation of 4-Chlorobenzoic Acid by Arthrobacter sp.

A mixed population, enriched and established in a defined medium, from a sewage sludge inoculum was capable of complete mineralization of 4-chlorobenzoate. An organism, identified as Arthrobacter sp., was isolated from the consortium and shown to be capable of utilizing 4-chlorobenzoate as the sole carbon and energy source in pure culture. This organism (strain TM-1), dehalogenated 4-chlorobenzoate as the initial step in the degradative pathway. The product, 4-hydroxybenzoate, was further metabolized via protocatechuate. The ability of strain TM-1 to degrade 4-chlorobenzoate in liquid medium at 25 degrees C was improved by the use of continuous culture and repeated sequential subculturing. Other chlorinated benzoates and the parent compound benzoate did not support growth of strain TM-1. An active cell extract was prepared and shown to dehalogenate 4-chloro-, 4-fluoro-, and 4-bromobenzoate. Dehalogenase activity had an optimum pH of 6.8 and an optimum temperature of 20 degrees C and was inhibited by dissolved oxygen and stimulated by manganese (Mn). Strain improvement resulted in an increase in the specific activity of the cell extract from 0.09 to 0.85 nmol of 4-hydroxybenzoate per min per mg of protein and a decrease in the doubling time of the organism from 50 to 1.6 h.

The origin of the oxygen incorporated during the dehalogenation/hydroxylation of 4-chlorobenzoate by an Arthrobacter sp.

An Arthrobacter sp. has been shown to dehalogenate 4-chlorobenzoate yielding 4-hydroxybenzoate. Experiments with 18O indicate that, in the presence of cell-free extracts, the hydroxyl group which is substituted onto the aromatic nucleus during dehalogenation is derived from water and not from molecular oxygen. Dehalogenation therefore is not catalysed by a mixed-function oxidase; instead a novel aromatic hydroxylase is implicated in the reaction.