ArticlePloS one2013
The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 61 citations in OpenAlex.
- Unveiling the molecular basis of arsenic resistance in Dietzia maris isolated from arsenic-contaminated soil.BMC biotechnology · 2026Article
- The key to arsenic pollution remediation: engineering and functional effects of arsenic-resistant microorganisms.World journal of microbiology & biotechnology · 2026Review
- Microbially mediated silicon-based agro-wastes: a possible option in reducing bioaccumulation of arsenic.Frontiers in nutrition · 2025Review
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Article
- Arsenic and Microorganisms: Genes, Molecular Mechanisms, and Recent Advances in Microbial Arsenic Bioremediation.Microorganisms · 2023Review
- The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. strain NT-26 and its native electron acceptor cytochrome cActa crystallographica. Section D, Structural biology · 2023Article
- In silico analysis of phylogeny, structure, and function of arsenite oxidase from unculturable microbiome of arsenic contaminated soil.Journal, genetic engineering & biotechnology · 2021Article
- Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: a case study with periplasmic nitrate reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- Molybdenum-Containing Enzymes.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Unraveling the inner workings of respiratory arsenate reductase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural and mechanistic analysis of the arsenate respiratory reductase provides insight into environmental arsenic transformations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Expression of the arsenite oxidation regulatory operon in Rhizobium sp. str. NT-26 is under the control of two promoters that respond to different environmental cues.MicrobiologyOpen · 2018Article
- A new family of periplasmic-binding proteins that sense arsenic oxyanions.Scientific reports · 2018Article
- Article
- Electron transfer through arsenite oxidase: Insights into Rieske interaction with cytochrome c.Biochimica et biophysica acta. Bioenergetics · 2017Article
- The active site structure and catalytic mechanism of arsenite oxidase.Scientific reports · 2017Article
- Structural and mechanistic insights on nitrate reductases.Protein science : a publication of the Protein Society · 2015Review
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Authors and funding
11 authors at 6 institutions in 4 countries.
Funding
Abstract
The arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate. The enzyme from the distantly related heterotroph, Alcaligenes faecalis, which is thought to oxidise arsenite for detoxification, consists of a large α subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small β subunit (AioB) which contains a Rieske 2Fe-2S cluster. The successful heterologous expression of the NT-26 Aio in Escherichia coli has resulted in the solution of its crystal structure. The NT-26 Aio, a heterotetramer, shares high overall similarity to the heterodimeric arsenite oxidase from A. faecalis but there are striking differences in the structure surrounding the Rieske 2Fe-2S cluster which we demonstrate explains the difference in the observed redox potentials (+225 mV vs. +130/160 mV, respectively). A combination of site-directed mutagenesis and electron paramagnetic resonance was used to explore the differences observed in the structure and redox properties of the Rieske cluster. In the NT-26 AioB the substitution of a serine (S126 in NT-26) for a threonine as in the A. faecalis AioB explains a -20 mV decrease in redox potential. The disulphide bridge in the A. faecalis AioB which is conserved in other betaproteobacterial AioB subunits and the Rieske subunit of the cytochrome bc 1 complex is absent in the NT-26 AioB subunit. The introduction of a disulphide bridge had no effect on Aio activity or protein stability but resulted in a decrease in the redox potential of the cluster. These results are in conflict with previous data on the betaproteobacterial AioB subunit and the Rieske of the bc 1 complex where removal of the disulphide bridge had no effect on the redox potential of the former but a decrease in cluster stability was observed in the latter.
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