Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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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, Moon-Joo (Department of Chemistry, Chosun University) ;
  • Kim, Chun-Sung (Research Center for Proteineous Materials, Chosun University) ;
  • Kim, Yun-A (Research Center for Proteineous Materials, Chosun University) ;
  • Choi, Hack-Sun (Research Center for Proteineous Materials, Chosun University) ;
  • Cho, Eun-Hee (Department of Biology Education, Chosun University) ;
  • Kim, Eung-Bin (Department of Biology, Yonsei University) ;
  • Kim, Young-Min (Department of Biology, Yonsei University) ;
  • Kim, Si-Wouk (Research Center for Proteineous Materials, Chosun University)
  • Published : 2002.06.01
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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, $c_L\;and\;c_H$, 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 $c_L$was higher than that from MDH to cytochrome $c_H$, indicating that the physiological primary electron acceptor for MDH is cytochrome $c_L$. 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 $c_L$ 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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