Crystal Structure of the 100 kDa Arsenite Oxidase from Alcaligenes faecalis in Two Crystal Forms at 1.64 Å and 2.03 Å

Ellis, P.J.; Conrads, Thomas P.; Hille, Russ; Kühn, Peter

doi:10.1016/s0969-2126(01)00566-4

Cited by 281 publications

(300 citation statements)

References 30 publications

(2 reference statements)

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“…This enzyme is a heterodimeric protein composed of a small subunit containing a Rieske [2Fe-2S] cluster and a large molybdopterin subunit, harboring a [3Fe-4S] cluster (Ellis et al, 2001). According to the previous studies and unified nomenclature proposed by Lett et al (2012), these subunits are encoded by aioB (small Rieske subunit, previously known as aoxA/aroB/asoB) and aioA (large molybdopyterin subunit, previously known as aoxB/aroA/asoB) genes.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional genomics of plasmid pSinA of Sinorhizobium sp. M14 encoding genes for the arsenite oxidation and arsenic resistance

Drewniak

Dziewit

Ciezkowska

et al. 2013

Journal of Biotechnology

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Plasmid pSinA of Sinorhizobium sp. M14 (Alphaproteobacteria) is the first described, natural, self-transferable plasmid harboring a complete set of genes for oxidation of arsenite. Removal of this plasmid from cells of the host strain caused the loss of resistance to arsenic and heavy metals (Cd, Co, Zn and Hg) and abolished the ability to grow on minimal salt medium supplemented with sodium arsenite as the sole energy source. Plasmid pSinA was introduced into other representatives of Alphaproteobacteria which resulted in acquisition of new abilities concerning arsenic resistance and oxidation, as well as heavy metals resistance. Microcosm experiments revealed that plasmid pSinA can also be transferred via conjugation into other indigenous bacteria from microbial community of As-contaminated soils, including representatives of Alpha-and Gammaproteobacteria. Analysis of "natural" transconjugants showed that pSinA is functional (expresses arsenite oxidase) and is stably maintained in their cells after approximately 60 generations of growth under nonselective conditions. This work clearly demonstrates that pSinA is a self-transferable, broad-host-range plasmid, which plays an important role in horizontal transfer of arsenic metabolism genes.

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Section: Introductionmentioning

confidence: 99%

Structural and functional genomics of plasmid pSinA of Sinorhizobium sp. M14 encoding genes for the arsenite oxidation and arsenic resistance

Drewniak

Dziewit

Ciezkowska

et al. 2013

Journal of Biotechnology

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“…The first crystal structure for a protein of this family was the one reported for DMSOR from Rhodobacter sphaeroides (6). Members of the DMSOR family share the Mo-containing ␣-subunit, such as DMSOR (6)(7)(8), formate dehydrogenase (FDH)-H (9), and dissimilatory nitrate reductase (NIR) (10), but may also have one or two additional small subunits as observed in arsenite oxidase (11) and in tungsten-containing FDH-T (12) (␣-and ␤-subunits), and in NIR A (NARGHI) (13) and FDH-N (14) (␣-, ␤-, and ␥-subunits). The only protein ligand to the Mo ion is either a Ser (DMSOR, TH), Cys (dissimilatory NIR), Asp (NIR A), or seleno-Cys (FDHs).…”

mentioning

confidence: 99%

“…The only protein ligand to the Mo ion is either a Ser (DMSOR, TH), Cys (dissimilatory NIR), Asp (NIR A), or seleno-Cys (FDHs). Arsenite oxidase is unique in having no covalent linkage between the protein and the Mo atom (11). All of these enzymes function as typical Mo hydroxylases, with the Mo ion cycling between Mo(IV) and Mo(VI) during catalytic turnover.…”

mentioning

confidence: 99%

Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols

Messerschmidt

Niessen

Abt

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalousdiffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalousdiffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)2 site in the ␣-subunit, and three [4FeO4S] centers in the ␤-subunit. The latter subunit carries a seven-stranded, mainly antiparallel ␤-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.

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“…The large subunit (AroA~90 kDa) of the arsenite oxidase is the first example of a new subgroup of the dimethylsulfoxide (DMSO) reductase family of molybdoenzymes (Ellis et al, 2001). It is reported that this heterodimeric enzyme is located on the outer surface of the inner membrane, and is transported to the cytoplasmic membrane (Lebrun et al, 2003).…”

Section: As(iii)-oxidizing Bacteriamentioning

confidence: 99%

Arsenic redox transformation by Pseudomonas sp. HN-2 isolated from arsenic-contaminated soil in Hunan, China

Zhang

Yin

Cai

et al. 2016

Journal of Environmental Sciences

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A mesophilic, Gram-negative, arsenite[As(III)]-oxidizing and arsenate[As(V)]-reducing bacterial strain, Pseudomonas sp. HN-2, was isolated from an As-contaminated soil. Phylogenetic analysis based on 16S rRNA gene sequencing indicated that the strain was closely related to Pseudomonas stutzeri. Under aerobic conditions, this strain oxidized 92.0% (61.4 μmol/L) of arsenite to arsenate within 3 hr of incubation. Reduction of As(V) to As(III) occurred in anoxic conditions. Pseudomonas sp. HN-2 is among the first soil bacteria shown to be capable of both aerobic As(III) oxidation and anoxic As(V) reduction. The strain, as an efficient As(III) oxidizer and As(V) reducer in Pseudomonas, has the potential to impact arsenic mobility in both anoxic and aerobic environments, and has potential application in As remediation processes.

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Crystal Structure of the 100 kDa Arsenite Oxidase from Alcaligenes faecalis in Two Crystal Forms at 1.64 Å and 2.03 Å

Cited by 281 publications

References 30 publications

Structural and functional genomics of plasmid pSinA of Sinorhizobium sp. M14 encoding genes for the arsenite oxidation and arsenic resistance

Structural and functional genomics of plasmid pSinA of Sinorhizobium sp. M14 encoding genes for the arsenite oxidation and arsenic resistance

Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols

Arsenic redox transformation by Pseudomonas sp. HN-2 isolated from arsenic-contaminated soil in Hunan, China

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