ArxA, a new clade of arsenite oxidase within the DMSO reductase family of molybdenum oxidoreductases
Abstract
Arsenotrophy, growth coupled to autotrophic arsenite oxidation or arsenate respiratory reduction, occurs only in the prokaryotic domain of life. The enzymes responsible for arsenotrophy belong to distinct clades within the DMSO reductase family of molybdenum-containing oxidoreductases: specifically arsenate respiratory reductase, ArrA, and arsenite oxidase, AioA (formerly referred to as AroA and AoxB). A new arsenite oxidase clade, ArxA, represented by the haloalkaliphilic bacterium Alkalilimnicola ehrlichii strain MLHE-1 was also identified in the photosynthetic purple sulfur bacterium Ectothiorhodospira sp. strain PHS-1. A draft genome sequence of PHS-1 was completed and an arx operon similar to MLHE-1 was identified. Gene expression studies showed that arxA was strongly induced with arsenite. Microbial ecology investigation led to the identification of additional arxA-like sequences in Mono Lake and Hot Creek sediments, both arsenic-rich environments in California. Phylogenetic analyses placed these sequences as distinct members of the ArxA clade of arsenite oxidases. ArxA-like sequences were also identified in metagenome sequences of several alkaline microbial mat environments of Yellowstone National Park hot springs. These results suggest that ArxA-type arsenite oxidases appear to be widely distributed in the environment presenting an opportunity for further investigations of the contribution of Arx-dependent arsenotrophy to the arsenic biogeochemical cycle.
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Krafft, T., & Macy, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550647.x · Cited by 230 · see citing works
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The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works
Earth Abides Arsenic Biotransformations
Zhu, Y.-G., Yoshinaga, M., Zhao, F.-J., & Rosen, B. P. (2014) · Annual Review of Earth and Planetary Sciences · doi:10.1146/annurev-earth-060313-054942 · Cited by 550 · see citing works
Glodowska, M., Stopelli, E., Schneider, M., Lightfoot, A., Rathi, B., Straub, D., Patzner, M., Duyen, V. T., AdvectAs Team Members, Berg, M., et al. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b07183 · Cited by 91 · see citing works
- Authors
- Zargar, K., Conrad, A., Bernick, D. L., Lowe, T. M., Stolc, V., Hoeft, S., Oremland, R. S., Stolz, J., & Saltikov, C. W.
- Affiliations
- University of California, Santa Cruz (US)
- United States Geological Survey (US)
- Duquesne University (US)
- Corresponding author
- Saltikov, Chad W.
- Venue
- Environmental Microbiology
- Publisher
- Wiley
- Published
- 2012-03-09
- Volume
- 14
- Issue
- 7
- Pages
- 1635-1645
- ISSN
- 1462-2912 (ISSN-L)
- 1462-2920
- OpenAlex
- W1772751970
- Cited by
- 150
- References
- 1
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 11 · 2023: 9 · 2022: 12 · 2021: 22 · 2020: 11 · 2019: 13 · 2018: 9 · 2017: 11 · 2016: 6 · 2015: 7 · 2014: 15 · 2013: 10 · 2012: 3
- FWCI
- 8.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Environmental Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Aeronautics and Space Administration
- U.S. Geological Survey
- Topics
- Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
- Physical Sciences › Engineering › Biomedical Engineering › Metal Extraction and Bioleaching
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Keywords
- arsenite oxidase, Ectothiorhodospira, arsenic biogeochemical cycle, haloalkaliphilic bacteria, purple sulfur bacteria, microbial mats, hot springs, metagenomics, phylogenetic analysis
- MeSH terms
- Arsenic, California, Genes, Bacterial, Iron-Sulfur Proteins, Operon, Oxidation-Reduction, Oxidoreductases, Phylogeny, Sequence Analysis, DNA, Ectothiorhodospira, Hot Springs, Autotrophic Processes, Arsenate Reductases, Metagenome
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