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Title: Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations

Abstract

Significance Microbial arsenate respiration enhances the mobility of arsenic and contributes to the poisoning of tens of millions of people worldwide. Our ability to quantitatively predict how microbial activities shape arsenic geochemistry depends on a detailed understanding of how the enzymes that catalyze arsenate reduction work under environmentally relevant conditions. The structural and kinetic findings of the Arr enzyme complex reported here both help rationalize its extracytoplasmic localization and allow us to predict that the rate of arsenate release from minerals likely constrains its activity in sedimentary environments. Moreover, this work illustrates that engineering environmental bacteria to overexpress their native proteins can be straightforward, a strategy that may advance the study of enzymes that are challenging to express in traditional hosts.

Authors:
 [1];  [2];  [3];  [3];  [4]
  1. Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125,
  2. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125,
  3. Institute of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, United Kingdom,
  4. Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125,, Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1464330
Grant/Contract Number:  
AC02-05CH11231
Resource Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Volume: 115 Journal Issue: 37; Journal ID: ISSN 0027-8424
Publisher:
Proceedings of the National Academy of Sciences
Country of Publication:
United States
Language:
English

Citation Formats

Glasser, Nathaniel R., Oyala, Paul H., Osborne, Thomas H., Santini, Joanne M., and Newman, Dianne K. Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations. United States: N. p., 2018. Web. doi:10.1073/pnas.1807984115.
Glasser, Nathaniel R., Oyala, Paul H., Osborne, Thomas H., Santini, Joanne M., & Newman, Dianne K. Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations. United States. https://doi.org/10.1073/pnas.1807984115
Glasser, Nathaniel R., Oyala, Paul H., Osborne, Thomas H., Santini, Joanne M., and Newman, Dianne K. Mon . "Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations". United States. https://doi.org/10.1073/pnas.1807984115.
@article{osti_1464330,
title = {Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations},
author = {Glasser, Nathaniel R. and Oyala, Paul H. and Osborne, Thomas H. and Santini, Joanne M. and Newman, Dianne K.},
abstractNote = {Significance Microbial arsenate respiration enhances the mobility of arsenic and contributes to the poisoning of tens of millions of people worldwide. Our ability to quantitatively predict how microbial activities shape arsenic geochemistry depends on a detailed understanding of how the enzymes that catalyze arsenate reduction work under environmentally relevant conditions. The structural and kinetic findings of the Arr enzyme complex reported here both help rationalize its extracytoplasmic localization and allow us to predict that the rate of arsenate release from minerals likely constrains its activity in sedimentary environments. Moreover, this work illustrates that engineering environmental bacteria to overexpress their native proteins can be straightforward, a strategy that may advance the study of enzymes that are challenging to express in traditional hosts.},
doi = {10.1073/pnas.1807984115},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 37,
volume = 115,
place = {United States},
year = {Mon Aug 13 00:00:00 EDT 2018},
month = {Mon Aug 13 00:00:00 EDT 2018}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1073/pnas.1807984115

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Cited by: 48 works
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