Cited by 160Arsenic contamination and mitigationMetal Extraction and BioleachingMicrobial metabolism and enzyme function

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Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor

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vanden Hoven, Rachel N, Santini, Joanne M·2004·Biochimica et Biophysica Acta (BBA) - Bioenergetics

Abstract

Heterotrophic arsenite oxidation by Hydrogenophaga sp. str. NT-14 is coupled to the reduction of oxygen and appears to yield energy for growth. Purification and partial characterization of the arsenite oxidase revealed that it (1). contains two heterologous subunits, AroA (86 kDa) and AroB (16 kDa), (2). has a native molecular mass of 306 kDa suggesting an alpha(3)beta(3) configuration, and (3). contains molybdenum and iron as cofactors. Although the Hydrogenophaga sp. str. NT-14 arsenite oxidase shares similarities to the arsenite oxidases purified from NT-26 and Alcaligenes faecalis, it differs with respect to activity and overall conformation. A c-551-type cytochrome was purified from Hydrogenophaga sp. str. NT-14 and appears to be the physiological electron acceptor for the arsenite oxidase. The cytochrome can also accept electrons from the purified NT-26 arsenite oxidase. A hypothetical electron transport chain for heterotrophic arsenite oxidation is proposed.

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Metadata

Authors
vanden Hoven, R. N., & Santini, J. M.
Affiliations
La Trobe University (AU)
Corresponding author
Santini, Joanne M
Venue
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher
Elsevier BV
Published
2004-06
Volume
1656
Issue
2-3
Pages
148-155
ISSN
0005-2728 (ISSN-L)
OpenAlex
W1967636082
Cited by
160
References
1
Citations by year
2026: 2 · 2025: 7 · 2024: 7 · 2023: 5 · 2022: 6 · 2021: 13 · 2020: 13 · 2019: 5 · 2018: 7 · 2017: 13 · 2016: 5 · 2015: 12 · 2014: 13 · 2013: 8 · 2012: 7
FWCI
3.64
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
Australian Research Council
Topics
  • Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
  • Physical Sciences › Materials Science › Metals and Alloys › Metal Extraction and Bioleaching
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Keywords
arsenite oxidase, aroA, molybdenum cofactor, iron cofactor, cytochrome c551, electron transport chain, oxygen reduction reaction, Alcaligenes faecalis, enzyme purification
MeSH terms
Amino Acid Sequence, Electron Transport, Electrophoresis, Polyacrylamide Gel, Iron, Molecular Sequence Data, Molecular Weight, Molybdenum, Oxidation-Reduction, Oxidoreductases, Oxygen, Protein Conformation, Sequence Homology, Amino Acid, Sequence Analysis, Protein, Protein Subunits, Comamonadaceae, Cytochromes c

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CoChat. (2026). Citation check: Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor. https://app.cochat.ai/papers/10.1016/j.bbabio.2004.03.001
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vanden Hoven, R. N., & Santini, J. M. (2004). Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor. Biochimica et Biophysica Acta (BBA) - Bioenergetics. https://doi.org/10.1016/j.bbabio.2004.03.001