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Journal of Bacteriology, December 2001, p. 6832-6840, Vol. 183, No. 23
Department of Microbiology, Iowa State
University, Ames, Iowa 50011
Received 17 May 2001/Accepted 11 September 2001
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.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.23.6832-6840.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Membrane-Associated Quinoprotein Formaldehyde
Dehydrogenase from Methylococcus capsulatus Bath


*
Corresponding author. Mailing address: Department of
Microbiology, Iowa State University, 205 Science Building, Ames, IA
50011-3211. Phone: (515) 294-2944. Fax: (515) 294-6019. E-mail:
aland{at}iastate.edu.
Present address: National Swine Research Center, USDA-ARS, Ames, IA
50011-3211.
Present address: Black Hills State University, Spearfish, SD
57799-9003.
§
Present address: Department of Chemistry and Biochemistry, Utah
State University, Logan, UT 84322-0300.
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