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Journal of Bacteriology, April 1999, p. 2142-2147, Vol. 181, No. 7
Department of Life Science,
Received 9 November 1998/Accepted 13 January 1999
Ferric iron reductase was purified from magnetotactic bacterium
Magnetospirillum (formerly Aquaspirillum)
magnetotacticum (ATCC 31632) to an electrophoretically
homogeneous state. The enzyme was loosely bound on the cytoplasmic face
of the cytoplasmic membrane and was found more frequently in magnetic
cells than in nonmagnetic cells. The molecular mass of the purified
enzyme was calculated upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be about 36 kDa, almost the same as that calibrated by gel filtration analysis. The enzyme required NADH and flavin mononucleotide (FMN) as optimal electron donor and cofactor,
respectively, and the activity was strongly inhibited by
Zn2+ acting as a partial mixed-type inhibitor. The
Km values for NADH and FMN were 4.3 and 0.035 µM, respectively, and the Ki values for
Zn2+ were 19.2 and 23.9 µM for NADH and FMN,
respectively. When the bacterium was grown in the presence of
ZnSO4, the magnetosome number in the cells and the ferric
iron reductase activity declined in parallel with an increase in the
ZnSO4 concentration of the medium, suggesting that the
ferric iron reductase purified in the present study may participate in
magnetite synthesis.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Iron Reductase for Magnetite Synthesis in the
Magnetotactic Bacterium Magnetospirillum
magnetotacticum
*
Corresponding author. Mailing address: Department of
Biology, Faculty of Science, Kanazawa University, Kakuma-machi,
Kanazawa 920-1192, Japan. Phone: 81-76-264-5719. Fax: 81-76-264-5918. E-mail: fukumor{at}kenroku.kanazawa-u.ac.jp.
Journal of Bacteriology, April 1999, p. 2142-2147, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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