Open AccessMethanol oxidation in a spontaneous mutant of Thiosphaera pantotropha with a methanol‐positive phenotype is catalysed by a dye‐linked ethanol dehydrogenase
Author(s) -
Ras Joyce,
Hazelaar Marten J,
Robertson Lesley A,
Kuenen J. Gijs,
Spanning Rob J.M,
Stouthamer Adriaan H,
Harms Nellie
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07467.x
Subject(s) - methanol dehydrogenase , methanol , chemistry , alcohol oxidoreductase , alcohol dehydrogenase , electron acceptor , ethanol , biochemistry , branched chain alpha keto acid dehydrogenase complex , mutant , dehydrogenase , enzyme , protein subunit , cytochrome , microbiology and biotechnology , photochemistry , biology , nad+ kinase , gene , organic chemistry
A spontaneous Thiosphaera pantotropha mutant (Tp9002) that is able to grow on methanol has been isolated. With hybridization experiments it has been demonstrated that mxaF , the gene encoding the large subunit of methanol dehydrogenase, is absent from T. pantotropha . In Tp9002, a dye‐linked enzyme activity was found with a substrate specificity similar to that of the dye‐linked ethanol dehydrogenase from Pseudomonas aeruginosa . The N‐terminus of a 26‐kDa cytochrome c , exclusively synthesized in Tp9002, is homologous to the N‐terminus of the electron acceptor of ethanol dehydrogenase. These results suggest that in Tp9002 a dye‐linked ethanol dehydrogenase is responsible for methanol oxidation, using a 26‐kDa cytochrome c as electron acceptor.