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Review
, 20 (13)

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

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Review

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

Jose María Miralles-Robledillo et al. Int J Mol Sci.

Abstract

Dimethyl sulfoxide reductases (DMSO) are molybdoenzymes widespread in all domains of life. They catalyse not only redox reactions, but also hydroxylation/hydration and oxygen transfer processes. Although literature on DMSO is abundant, the biological significance of these enzymes in anaerobic respiration and the molecular mechanisms beyond the expression of genes coding for them are still scarce. In this review, a deep revision of the literature reported on DMSO as well as the use of bioinformatics tools and free software has been developed in order to highlight the relevance of DMSO reductases on anaerobic processes connected to different biogeochemical cycles. Special emphasis has been addressed to DMSO from extremophilic organisms and their role in nitrogen cycle. Besides, an updated overview of phylogeny of DMSOs as well as potential applications of some DMSO reductases on bioremediation approaches are also described.

Keywords: MoCo cofactor; N-cycle; biogeochemical cycles; dimethyl sulfoxide reductases; nitrate reductase; perchlorate reductase; phylogeny; redox reactions.

Conflict of interest statement

The author declares no conflict of interest.

Figures

Figure 1
Figure 1
Molybdenum cofactors. (a) The iron-molybdenum cofactor (FeMoCo) of bacterial nitrogenases and (b) pyranopterin molecule from which the pterin-based cofactors (MoCo) are originated. Molecules drawn with BioVIA Draw 2019 [8].
Figure 2
Figure 2
Biosynthesis of the bis-molybdopterin-guanine dinucleotide (Bis-MGD) cofactor. 1 and 2: Transference of the sulfur atom to the cPMP by active MPT synthase and dissociation of MoaD/MoaE. 3: Association of MoaD with MoeB. 4: Restoration of thiocarboxylate group and dissociation of MoaD/MoeB. 5: Reassociation of MoaD/MoaE (with the thiocarboxylate group). Molecules drawn with BioVIA Draw 2019.
Figure 3
Figure 3
Reaction catalyzed by nitrate reductases. This is the first reaction in assimilatory nitrate reduction (catalyzed by Nas), Nitrate reductase (NR: eukNR, Nar, Nap, and Nas).
Figure 4
Figure 4
General scheme of perchlorate and chlorate reduction due to microbial activities. The first reaction is catalyzed by perchlorate reductases and the second one is catalyzed by chlorate reductases. Enzymes able to show both activities have also been described ((per)chlorate reductases).
Figure 5
Figure 5
Phylogenetic tree built with 155 sequences of the catalytic subunit from 10 respiratory-related enzymes belonging to the dimethyl sulfoxide reductases (DMSO) reductase family, together with a brief description (legend) of the organism from which each sequence belongs. Phylogenetic tree was built with Clustal Omega and iTol v4 software.
Figure 6
Figure 6
Clustal Omega alignment of halophilic respiratory nitrate reductases (NarG), TMAO reductases (TorA), and DMSO reductases (DmsA). In grey, aspartate which coordinates Mo atom in haloarchaeal NarG and DmsA aligned with possible coordination aspartate from haloarchaeal TorA.
Figure 7
Figure 7
Clustal Omega alignment of all PcrA proteins. Aspartate, which coordinates Mo atom, is in grey. Grey box represents the separate clade of PcrA in which their aspartate is not aligned with the aspartate from the two other groups of PcrA.
Figure 8
Figure 8
EMBOSS Needle alignment of PcrA (A. aryzae) with NarG (H. mediterranei). In grey are the residues of the hydrophobic tunnel of each enzyme. Trp461 from PcrA changes to Glutamate in NarG.
Figure 9
Figure 9
(a) Structure of the closed tunnel in PcrA from A. oryzae (PDB ID:4YDD). The gate residues F164, Y165, and W461 are shown in stick. (b) Model of NarG from H. mediterranei. The same positions of the hydrophobic tunnel in PcrA are showing in NarG structural model. W461 is substituted by E462 in the halophilic NarG. Blue: Nitrogen; Cyan; hydrogen; Red: oxygen.

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