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J. Biochem, 1976, Vol. 80, No. 1 79-87
© 1976 Japanese Biochemical Society

research-article

Purification and Properties of an Enzyme Catalyzing the Splitting of Carbon-Mercury Linkages from Mercury-Resistant Pseudomonas K-62 Strain

1. Splitting Enzyme 1

Toshiyuki TEZUKA and Kenzo TONOMURA

Fermentation Research Institute Inage, Chiba-shi, Chiba 281

An enzyme (S-1) which catalyzes the splitting of carbon-mercury linkages of organo-mercury compounds was purified about 24-fold from the cell-free extract of mercuryresistant Pseudomonas K-62 strain by treatment with streptomycin, precipitation with ammonium sulfate, and successive chromatography on Sephadex G-150, DEAE-Sephadex, and DEAE-cellulose. A purified preparation of the enzyme showed a single band on polyacrylamide gel electrophoresis, and was colorless. The molecular weight of the enzyme was estimated to be 19, 000, and Km was 5.3*10-5 M for p-chloromercuribenzoic acid (PCMB). The temperature and pH optimum for the reaction were 50° and 7.0, respectively. The enzyme was capable of catalyzing the decomposition of methylmercuric chloride (MMC), ethylmercuric chloride (EMC), phenylmercuric acetate (PMA), and PCMB in the presence of a sulfhydryl compound to form a mercuric ion plus methane, ethane, benzene, or benzoic acid, respectively. The mercuric ion thus formed was reduced to metallic mercury by metallic mercury-releasing enzyme (MMR-enzyme).


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M. Kiyono and H. Pan-Hou
The merG Gene Product Is Involved in Phenylmercury Resistance in Pseudomonas Strain K-62
J. Bacteriol., February 1, 1999; 181(3): 726 - 730.
[Abstract] [Full Text]


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