Properties of electron carriers in the process of methanol oxidation in a new restricted facultative marine methylotrophic bacterium, Methylophaga sp. MP

Moonjoo Koh, Chun Sung Kim, Yun A. Kim, Hack Sun Choi, Eun Hee Cho, Eungbin Kim, Young Min Kim, Si Wouk Kim

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Methanol dehydrogenase (MDH) and c-type cytochromes from marine methanol-oxidizing bacterium, Methylophaga sp. MP, were purified and characterized. The native MDH had a molecular mass of 148 kDa and its isoelectric point was 5.5. Two c-type cytochromes, cL and cH, were found, and their isoelectric points were 3.4 and 8.0, respectively. The purified MDH had higher thermal stability than that of the other soil methylotrophic bacteria. The electron flow rate from MDH to cytochrome cL was higher than that from MDH to cytochrome CH, indicating that the physiological primary electron acceptor for MDH is cytochrome CL. The electron transfer from MDH to phenazine ethosulfate (PES, artificial electron acceptor) in the two dye (PES/DCPIP)-linked assay system was not inhibited by NaCl, whereas the electron flow from MDH to cytochrome CL in the cytochrome/ DCPIP-linked assay system was suppressed significantly by NaCl. Metal chelating agents such as EDTA showed the same effects on the MDH activity.

Original languageEnglish
Pages (from-to)476-482
Number of pages7
JournalJournal of microbiology and biotechnology
Volume12
Issue number3
Publication statusPublished - 2002 Jul 30

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Methanol
Electrons
Bacteria
Isoelectric Point
Cytochromes
Cytochrome c Group
alcohol dehydrogenase (acceptor)
Chelating Agents
Edetic Acid
Coloring Agents
Soil
Hot Temperature
cytochrome C(L)

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Koh, Moonjoo ; Kim, Chun Sung ; Kim, Yun A. ; Choi, Hack Sun ; Cho, Eun Hee ; Kim, Eungbin ; Kim, Young Min ; Kim, Si Wouk. / Properties of electron carriers in the process of methanol oxidation in a new restricted facultative marine methylotrophic bacterium, Methylophaga sp. MP. In: Journal of microbiology and biotechnology. 2002 ; Vol. 12, No. 3. pp. 476-482.
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abstract = "Methanol dehydrogenase (MDH) and c-type cytochromes from marine methanol-oxidizing bacterium, Methylophaga sp. MP, were purified and characterized. The native MDH had a molecular mass of 148 kDa and its isoelectric point was 5.5. Two c-type cytochromes, cL and cH, were found, and their isoelectric points were 3.4 and 8.0, respectively. The purified MDH had higher thermal stability than that of the other soil methylotrophic bacteria. The electron flow rate from MDH to cytochrome cL was higher than that from MDH to cytochrome CH, indicating that the physiological primary electron acceptor for MDH is cytochrome CL. The electron transfer from MDH to phenazine ethosulfate (PES, artificial electron acceptor) in the two dye (PES/DCPIP)-linked assay system was not inhibited by NaCl, whereas the electron flow from MDH to cytochrome CL in the cytochrome/ DCPIP-linked assay system was suppressed significantly by NaCl. Metal chelating agents such as EDTA showed the same effects on the MDH activity.",
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Properties of electron carriers in the process of methanol oxidation in a new restricted facultative marine methylotrophic bacterium, Methylophaga sp. MP. / Koh, Moonjoo; Kim, Chun Sung; Kim, Yun A.; Choi, Hack Sun; Cho, Eun Hee; Kim, Eungbin; Kim, Young Min; Kim, Si Wouk.

In: Journal of microbiology and biotechnology, Vol. 12, No. 3, 30.07.2002, p. 476-482.

Research output: Contribution to journalArticle

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T1 - Properties of electron carriers in the process of methanol oxidation in a new restricted facultative marine methylotrophic bacterium, Methylophaga sp. MP

AU - Koh, Moonjoo

AU - Kim, Chun Sung

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AU - Choi, Hack Sun

AU - Cho, Eun Hee

AU - Kim, Eungbin

AU - Kim, Young Min

AU - Kim, Si Wouk

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N2 - Methanol dehydrogenase (MDH) and c-type cytochromes from marine methanol-oxidizing bacterium, Methylophaga sp. MP, were purified and characterized. The native MDH had a molecular mass of 148 kDa and its isoelectric point was 5.5. Two c-type cytochromes, cL and cH, were found, and their isoelectric points were 3.4 and 8.0, respectively. The purified MDH had higher thermal stability than that of the other soil methylotrophic bacteria. The electron flow rate from MDH to cytochrome cL was higher than that from MDH to cytochrome CH, indicating that the physiological primary electron acceptor for MDH is cytochrome CL. The electron transfer from MDH to phenazine ethosulfate (PES, artificial electron acceptor) in the two dye (PES/DCPIP)-linked assay system was not inhibited by NaCl, whereas the electron flow from MDH to cytochrome CL in the cytochrome/ DCPIP-linked assay system was suppressed significantly by NaCl. Metal chelating agents such as EDTA showed the same effects on the MDH activity.

AB - Methanol dehydrogenase (MDH) and c-type cytochromes from marine methanol-oxidizing bacterium, Methylophaga sp. MP, were purified and characterized. The native MDH had a molecular mass of 148 kDa and its isoelectric point was 5.5. Two c-type cytochromes, cL and cH, were found, and their isoelectric points were 3.4 and 8.0, respectively. The purified MDH had higher thermal stability than that of the other soil methylotrophic bacteria. The electron flow rate from MDH to cytochrome cL was higher than that from MDH to cytochrome CH, indicating that the physiological primary electron acceptor for MDH is cytochrome CL. The electron transfer from MDH to phenazine ethosulfate (PES, artificial electron acceptor) in the two dye (PES/DCPIP)-linked assay system was not inhibited by NaCl, whereas the electron flow from MDH to cytochrome CL in the cytochrome/ DCPIP-linked assay system was suppressed significantly by NaCl. Metal chelating agents such as EDTA showed the same effects on the MDH activity.

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