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Biodegradation

BTI1, an Azoreductase with pH-Dependent Substrate Specificity

Hans E. Johansson, Mary K. Johansson, Albert C. Wong, Eliana S. Armstrong, Erik J. Peterson, Richard E. Grant, Margaret A. Roy, Mark V. Reddington, Ronald M. Cook
Hans E. Johansson
Biosearch Technologies, Inc., 81 Digital Drive, Novato, California 94949-5728
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Mary K. Johansson
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Albert C. Wong
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Eliana S. Armstrong
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Erik J. Peterson
§Present address: Department of Psychology, Colorado State University, Fort Collins, CO.
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Richard E. Grant
¶Present address: University of Wisconsin Biotechnology Center, Madison, WI.
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Margaret A. Roy
‖Present address: Complete Genomics, Inc., Mountain View, CA.
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Mark V. Reddington
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Ronald M. Cook
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DOI: 10.1128/AEM.02289-10
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ABSTRACT

The group II azoreductase BTI1 utilizes NADPH to directly cleave azo bonds in water-soluble azo dyes, including quenchers of fluorescence. Unexpectedly, optimal reduction was dye specific, ranging from a pH of <5.5 for Janus green B, to pH 6.0 for methyl red, methyl orange, and BHQ-10, to pH >8.3 for flame orange.

FOOTNOTES

    • Received 24 September 2010.
    • Accepted 8 April 2011.
    • Accepted manuscript posted online 29 April 2011.
  • ↵† Supplemental material for this article may be found at http://dx.doi.org/10.1128/AEM.02289-10.

  • Copyright © 2011, American Society for Microbiology. All Rights Reserved.
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BTI1, an Azoreductase with pH-Dependent Substrate Specificity
Hans E. Johansson, Mary K. Johansson, Albert C. Wong, Eliana S. Armstrong, Erik J. Peterson, Richard E. Grant, Margaret A. Roy, Mark V. Reddington, Ronald M. Cook
Applied and Environmental Microbiology Jun 2011, 77 (12) 4223-4225; DOI: 10.1128/AEM.02289-10

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BTI1, an Azoreductase with pH-Dependent Substrate Specificity
Hans E. Johansson, Mary K. Johansson, Albert C. Wong, Eliana S. Armstrong, Erik J. Peterson, Richard E. Grant, Margaret A. Roy, Mark V. Reddington, Ronald M. Cook
Applied and Environmental Microbiology Jun 2011, 77 (12) 4223-4225; DOI: 10.1128/AEM.02289-10
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