Characterization of methylamine dehydrogenase from Bacterium W3A1. Interaction with reductants and amino-containing compounds

Methylamine dehydrogenase from bacterium W3A1 is composed of two subunits of unequal molecular weight. From sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a molecular weight of 45,000 is obtained for the larger subunit and 15,500 for the smaller one. Gel chromatography of the native enzy...

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Bibliographic Details
Published in:Biochemistry (Easton) 1983-08, Vol.22 (16), p.3858-3868
Main Authors: Kenney, William C, McIntire, William
Format: Article
Language:English
Subjects:
amine dehydrogenase
Anaerobiosis
bacteria
Bacteria - enzymology
Bacteriology
Biological and medical sciences
Dithionite - pharmacology
E.S.R
Electron Spin Resonance Spectroscopy
Fundamental and applied biological sciences. Psychology
Kinetics
Macromolecular Substances
Metabolism. Enzymes
Microbiology
Molecular Weight
Oxidoreductases Acting on CH-NH Group Donors - isolation & purification
Oxidoreductases Acting on CH-NH Group Donors - metabolism
redox properties
Spectrophotometry
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Summary:Methylamine dehydrogenase from bacterium W3A1 is composed of two subunits of unequal molecular weight. From sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a molecular weight of 45,000 is obtained for the larger subunit and 15,500 for the smaller one. Gel chromatography of the native enzyme yields a molecular weight of 127,000. These data suggest that the enzyme has a tetrameric structure of type A sub(2)B sub(2). The enzyme contains a chromophore, with absorbance maximum at 429 nm. Anaerobic titration of the enzyme with dithionite or methylamine results initially in an increase in absorbance at 429 nm which continues until 1 molar equiv of reductant is added. The enzyme at this stage has an electron spin resonance spectrum of 7.5 G width and a g value of 2.0086. Subsequent addition of reducing agent leads to a decrease in absorbance at 429 nm and a concomitant increase in absorbance at 330 nm. This process also consume 1 mol of reductant/mol of enzyme. The results are consistent with the titration of 2 mol of cofactor/mol of enzyme.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00285a022