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Effect of Deuteration on the Activity of Methanol Dehydrogenase from Methylophilus sp. B-7741

Effect of Deuteration on the Activity of Methanol Dehydrogenase from Methylophilus sp. B-7741 We studied the effect of deuterium oxide present in the medium on the activity of methanol dehydrogenase (EC 1.1.99.8) from methylotrophic bacteria Methylophilus sp. B-7741. Methanol dehydrogenase activity in extracts of the biomass obtained in a highly deuterated medium (2H-enzyme) was 34–47% of the enzyme activity in the control biomass (1H-enzyme), which depended on the reaction conditions. The isotopic effects of substrate deuterium (methanol) for 1H-enzyme and 2H-enzyme were 1.37 ± 0.05 and 1.38 ± 0.01, respectively. We revealed for the first time the reverse isotopic effect of solvent deuterium in the reaction catalyzed by methanol dehydrogenase (0.80 ± 0.02 and 0.60 ± 0.01 for 1H-enzyme and 2H-enzyme, respectively). http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Effect of Deuteration on the Activity of Methanol Dehydrogenase from Methylophilus sp. B-7741

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References (18)

Publisher
Springer Journals
Copyright
Copyright © 2004 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Medical Microbiology; Biochemistry, general; Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1023/B:ABIM.0000010344.54860.72
Publisher site
See Article on Publisher Site

Abstract

We studied the effect of deuterium oxide present in the medium on the activity of methanol dehydrogenase (EC 1.1.99.8) from methylotrophic bacteria Methylophilus sp. B-7741. Methanol dehydrogenase activity in extracts of the biomass obtained in a highly deuterated medium (2H-enzyme) was 34–47% of the enzyme activity in the control biomass (1H-enzyme), which depended on the reaction conditions. The isotopic effects of substrate deuterium (methanol) for 1H-enzyme and 2H-enzyme were 1.37 ± 0.05 and 1.38 ± 0.01, respectively. We revealed for the first time the reverse isotopic effect of solvent deuterium in the reaction catalyzed by methanol dehydrogenase (0.80 ± 0.02 and 0.60 ± 0.01 for 1H-enzyme and 2H-enzyme, respectively).

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Oct 18, 2004

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