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- W2033038412 abstract "ABSTRACT A membrane-associated, dye-linked formaldehyde dehydrogenase (DL-FalDH) was isolated from the obligate methylotroph Methylococcus capsulatus Bath. The enzyme was the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 μmol of Cu per mg of cell protein) copper medium and expressing the membrane-associated methane monooxygenase. Soluble NAD(P) + -linked formaldehyde oxidation was the major activity in cells cultured in low-copper medium and expressing the soluble methane monooxygenase (Tate and Dalton, Microbiology 145:159–167, 1999; Vorholt et al., J. Bacteriol. 180:5351–5356, 1998). The membrane-associated enzyme is a homotetramer with a subunit molecular mass of 49,500 Da. UV-visible absorption, electron paramagnetic resonance, and electrospray mass spectrometry suggest the redox cofactor of the DL-FalDH is pyrroloquinoline quinone (PQQ), with a PQQ-to-subunit stochiometry of approximately 1:1. The enzyme was specific for formaldehyde, oxidizing formaldehyde to formate, and utilized the cytochrome b 559/569 complex as the physiological electron acceptor." @default.
- W2033038412 created "2016-06-24" @default.
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- W2033038412 date "2001-12-01" @default.
- W2033038412 modified "2023-10-10" @default.
- W2033038412 title "Membrane-Associated Quinoprotein Formaldehyde Dehydrogenase from <i>Methylococcus capsulatus</i> Bath" @default.
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- W2033038412 doi "https://doi.org/10.1128/jb.183.23.6832-6840.2001" @default.
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