Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath

J. A. Zahn, D. J. Bergmann, J. M. Boyd, R. C. Kunz, A. A. DiSpirito

Research output: Contribution to journalArticle

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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 b559/569 complex as the physiological electron acceptor.

Original languageEnglish (US)
Pages (from-to)6832-6840
Number of pages9
JournalJournal of bacteriology
Volume183
Issue number23
DOIs
StatePublished - Nov 26 2001

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glutathione-independent formaldehyde dehydrogenase
Methylococcus capsulatus
methane monooxygenase
Baths
Formaldehyde
PQQ Cofactor
formic acid
Membranes
Enzymes
Copper
Cultured Cells
Coloring Agents
Electron Spin Resonance Spectroscopy
Microbiology
NAD
Oxidation-Reduction
Mass Spectrometry
Electrons

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Zahn, J. A. ; Bergmann, D. J. ; Boyd, J. M. ; Kunz, R. C. ; DiSpirito, A. A. / Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath. In: Journal of bacteriology. 2001 ; Vol. 183, No. 23. pp. 6832-6840.
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Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath. / Zahn, J. A.; Bergmann, D. J.; Boyd, J. M.; Kunz, R. C.; DiSpirito, A. A.

In: Journal of bacteriology, Vol. 183, No. 23, 26.11.2001, p. 6832-6840.

Research output: Contribution to journalArticle

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AU - Zahn, J. A.

AU - Bergmann, D. J.

AU - Boyd, J. M.

AU - Kunz, R. C.

AU - DiSpirito, A. A.

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N2 - 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 b559/569 complex as the physiological electron acceptor.

AB - 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 b559/569 complex as the physiological electron acceptor.

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