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MICROBIAL GROWTH ON C-1 COMPOUNDS. 6. OXIDATION OF METHANOL, FORMALDEHYDE AND FORMATE BY METHANOL-GROWN PSEUDOMONAS AM 1,
MEDICAL RESEARCH COUNCIL OXFORD (ENGLAND) CELL METABOLISM RESEARCH UNIT
The complete oxidation of methanol to carbon dioxide in cell-free extracts of methanol-grown Pseudomonas AM 1 was investigated. By using 3-amino-1,2,4-triazole, a known inhibitor of catalase, the independence of methanol oxidation from catalatic activity was shown. The only enzyme capable of oxidizing methanol that could be demonstrated was a dehydrogenase that can be linked to phenazine methosulphate and required the presence of NH4 ions. An aldehyde dehydrogenase that reduced 2,6-dichlorophenol-indophenol or phenazine methosulphate in the presence of formaldehyde was found in cell-free extracts and was purified. A nicotinamide-adenine nucleotidelinked formate dehydrogenase was found in cell-free extracts and purified. The possible significance of these enzymes in the oxidation of C-1 substrates by intact cells is discussed. Cell-free extracts of methanol-grown Protaminobacter ruber, Pseudomonas extroquens and Pseudomonas methanica have been found to possess a methanol dehydrogenases similar to those found in Pseudomonas AM 1. A specific nicotinamide-adenine dinucleotidelinked formaldehyde dehydrogenase was found in high activity in extracts of methanol-grown Pseudomonas methanica, in lower activity in extracts of methanolgrown Pseudomonas extorquens and Protaminobacter ruber.
Pub. in Biochemical Journal (Gt. Brit.) v93 p281-90 1964 (Copies available only to DDC users). See also AD-612 241.
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