Journal of Microbiology and Biotechnology

  • 제21권5호
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  • Pages.464-469
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  • 2011
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
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Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans

  • Mo, Hongyu (College of Biology, Hunan University) ;
  • Chen, Qian (College of Biology, Hunan University) ;
  • Du, Juan (College of Biology, Hunan University) ;
  • Tang, Lin (College of Biology, Hunan University) ;
  • Qin, Fang (College of Biology, Hunan University) ;
  • Miao, Bo (Department of Bioengineering, Central South University) ;
  • Wu, Xueling (Department of Bioengineering, Central South University) ;
  • Zeng, Jia (College of Biology, Hunan University)
  • 투고 : 2011.01.14
  • 심사 : 2011.03.11
  • 발행 : 2011.05.28
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초록

The arsH gene is one of the arsenic resistance system in bacteria and eukaryotes. The ArsH protein was annotated as a NADPH-dependent flavin mononucleotide (FMN) reductase with unknown biological function. Here we report for the first time that the ArsH protein showed high ferric reductase activity. Glu104 was an essential residue for maintaining the stability of the FMN cofactor. The ArsH protein may perform an important role for cytosolic ferric iron assimilation in vivo.

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참고문헌

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피인용 문헌

  1. Purification, crystallization and preliminary X‐ray diffraction analysis of ArsH from Synechocystis sp. strain PCC 6803 vol.70, pp.4, 2011, https://doi.org/10.1107/s2053230x14004865
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  5. A Model of Aerobic and Anaerobic Metabolism of Hydrogen in the Extremophile Acidithiobacillus ferrooxidans vol.11, pp.None, 2020, https://doi.org/10.3389/fmicb.2020.610836
  6. Molecular Mechanisms Underpinning Aggregation in Acidiphilium sp. C61 Isolated from Iron-Rich Pelagic Aggregates vol.8, pp.3, 2020, https://doi.org/10.3390/microorganisms8030314
  7. ArsH protects Pseudomonas putida from oxidative damage caused by exposure to arsenic vol.22, pp.6, 2011, https://doi.org/10.1111/1462-2920.14991