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Michael L. Wells

Publications and source records attributed to Michael L. Wells.

4 recordsLinked to original sources

Impact of the dimethyl sulfoxide reductase superfamily on the evolution of biogeochemical cycles

The dimethyl sulfoxide reductase (or MopB) family is a diverse assemblage of enzymes found throughout Bacteria and Archaea . Many of these enzymes are believed to have been present in the last universal common ancestor (LUCA) of all cellular lineages. However, gaps in knowledge remain about how MopB enzymes evolved and how this diversification of functions impacted global biogeochemical cycles through geologic time. In this study, we perform maximum likelihood phylogenetic analyses on manually curated comparative genomic and metagenomic data sets containing over 47,000 distinct MopB homologs. We demonstrate that these enzymes constitute a catalytically and mechanistically diverse superfamily defined not by the molybdopterin- or tungstopterin-containing [molybdopterin or tungstopterin bis (pyranopterin guanine dinucleotide) (Mo/W- bis PGD)] cofactor but rather by the structural fold that binds it in the protein. Our results suggest that major metabolic innovations were the result of the loss of the metal cofactor or the gain or loss of protein domains. Phylogenetic analyses also demonstrated that formate oxidation and CO 2 reduction were the ancestral functions of the superfamily, traits that have been vertically inherited from the LUCA. Nearly all of the other families, which drive all other biogeochemical cycles mediated by this superfamily, originated in the bacterial domain. Thus, organisms from Bacteria have been the key drivers of catalytic and biogeochemical innovations within the superfamily. The relative ordination of MopB families and their associated catalytic activities emphasize fundamental mechanisms of evolution in this superfamily. Furthermore, it underscores the importance of prokaryotic adaptability in response to the transition from an anoxic to an oxidized atmosphere.

Microbiology Spectrum

Respiratory selenite reductase from Bacillus selenitireducens strain MLS10

The putative respiratory selenite [Se(IV)] reductase (Srr) from Bacillus selenitireducens MLS10 has been identified through a polyphasic approach involving genomics, proteomics, and enzymology. Nondenaturing gel assays were used to identify Srr in cell fractions, and the active band was shown to contain a single protein of 80 kDa. The protein was identified through liquid chromatography-tandem mass spectrometry (LC-MS/MS) as a homolog of the catalytic subunit of polysulfide reductase (PsrA). It was found to be encoded as part of an operon that contains six genes that we designated srrE , srrA , s rrB , srrC , srrD , and srrF . SrrA is the catalytic subunit (80 kDa), with a twin-arginine translocation (TAT) leader sequence indicative of a periplasmic protein and one putative 4Fe-4S binding site. SrrB is a small subunit (17 kDa) with four putative 4Fe-4S binding sites, SrrC (43 kDa) is an anchoring subunit, and SrrD (24 kDa) is a chaperon protein. Both SrrE (38 kDa) and SrrF (45 kDa) were annotated as rhodanese domain-containing proteins. Phylogenetic analysis revealed that SrrA belonged to the PsrA/PhsA clade but that it did not define a distinct subgroup, based on the putative homologs that were subsequently identified from other known selenite-respiring bacteria (e.g., Desulfurispirillum indicum and Pyrobaculum aerophilum ). The enzyme appeared to be specific for Se(IV), showing no activity with selenate, arsenate, or thiosulfate, with a K m of 145 ± 53 μM, a V max of 23 ± 2.5 μM min −1 , and a k cat of 23 ± 2.68 s −1 . These results further our understanding of the mechanisms of selenium biotransformation and its biogeochemical cycle.

Journal of Bacteriology

Eocene and Miocene extension, meteoric fluid infiltration, and core complex formation in the Great Basin (Raft River Mountains, Utah)

Metamorphic core complexes (MCCs) in the North American Cordillera reflect the effects of lithospheric extension and contribute to crustal adjustments both during and after a protracted subduction history along the Pacific plate margin. While the Miocene-to-recent history of most MCCs in the Great Basin, including the Raft River-Albion-Grouse Creek MCC, is well documented, early Cenozoic tectonic fabrics are commonly severely overprinted. We present stable isotope, geochronological ( 40 Ar/ 39 Ar), and microstructural data from the Raft River detachment shear zone. Hydrogen isotope ratios of syntectonic white mica ( δ 2 H ms ) from mylonitic quartzite within the shear zone are very low (−90‰ to −154‰, Vienna SMOW) and result from multiphase synkinematic interaction with surface-derived fluids. 40 Ar/ 39 Ar geochronology reveals Eocene (re)crystallization of white mica with δ 2 H ms ≥ −154‰ in quartzite mylonite of the western segment of the detachment system. These δ 2 H ms values are distinctively lower than in localities farther east ( δ 2 H ms ≥ −125‰), where 40 Ar/ 39 Ar geochronological data indicate Miocene (18–15 Ma) extensional shearing and mylonitic fabric formation. These data indicate that very low δ 2 H surface-derived fluids penetrated the brittle-ductile transition as early as the mid-Eocene during a first phase of exhumation along a detachment rooted to the east. In the eastern part of the core complex, prominent top-to-the-east ductile shearing, mid-Miocene 40 Ar/ 39 Ar ages, and higher δ 2 H values of recrystallized white mica, indicate Miocene structural and isotopic overprinting of Eocene fabrics.

Utah