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[FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA

The use of [FeFe]-hydrogenase enzymes for the biotechnological production of H(2) or other reduced products has been limited by their sensitivity to oxygen (O(2)). Here, we apply a PCR-directed approach to determine the distribution, abundance, and diversity of hydA gene fragments along co-varying s...

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Autores principales: Boyd, Eric S., Hamilton, Trinity L., Swanson, Kevin D., Howells, Alta E., Baxter, Bonnie K., Meuser, Jonathan E., Posewitz, Matthew C., Peters, John W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284687/
https://www.ncbi.nlm.nih.gov/pubmed/25464382
http://dx.doi.org/10.3390/ijms151221947
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author Boyd, Eric S.
Hamilton, Trinity L.
Swanson, Kevin D.
Howells, Alta E.
Baxter, Bonnie K.
Meuser, Jonathan E.
Posewitz, Matthew C.
Peters, John W.
author_facet Boyd, Eric S.
Hamilton, Trinity L.
Swanson, Kevin D.
Howells, Alta E.
Baxter, Bonnie K.
Meuser, Jonathan E.
Posewitz, Matthew C.
Peters, John W.
author_sort Boyd, Eric S.
collection PubMed
description The use of [FeFe]-hydrogenase enzymes for the biotechnological production of H(2) or other reduced products has been limited by their sensitivity to oxygen (O(2)). Here, we apply a PCR-directed approach to determine the distribution, abundance, and diversity of hydA gene fragments along co-varying salinity and O(2) gradients in a vertical water column of Great Salt Lake (GSL), UT. The distribution of hydA was constrained to water column transects that had high salt and relatively low O(2) concentrations. Recovered HydA deduced amino acid sequences were enriched in hydrophilic amino acids relative to HydA from less saline environments. In addition, they harbored interesting variations in the amino acid environment of the complex H-cluster metalloenzyme active site and putative gas transfer channels that may be important for both H(2) transfer and O(2) susceptibility. A phylogenetic framework was created to infer the accessory cluster composition and quaternary structure of recovered HydA protein sequences based on phylogenetic relationships and the gene contexts of known complete HydA sequences. Numerous recovered HydA are predicted to harbor multiple N- and C-terminal accessory iron-sulfur cluster binding domains and are likely to exist as multisubunit complexes. This study indicates an important role for [FeFe]-hydrogenases in the functioning of the GSL ecosystem and provides new target genes and variants for use in identifying O(2) tolerant enzymes for biotechnological applications.
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spelling pubmed-42846872015-01-21 [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA Boyd, Eric S. Hamilton, Trinity L. Swanson, Kevin D. Howells, Alta E. Baxter, Bonnie K. Meuser, Jonathan E. Posewitz, Matthew C. Peters, John W. Int J Mol Sci Article The use of [FeFe]-hydrogenase enzymes for the biotechnological production of H(2) or other reduced products has been limited by their sensitivity to oxygen (O(2)). Here, we apply a PCR-directed approach to determine the distribution, abundance, and diversity of hydA gene fragments along co-varying salinity and O(2) gradients in a vertical water column of Great Salt Lake (GSL), UT. The distribution of hydA was constrained to water column transects that had high salt and relatively low O(2) concentrations. Recovered HydA deduced amino acid sequences were enriched in hydrophilic amino acids relative to HydA from less saline environments. In addition, they harbored interesting variations in the amino acid environment of the complex H-cluster metalloenzyme active site and putative gas transfer channels that may be important for both H(2) transfer and O(2) susceptibility. A phylogenetic framework was created to infer the accessory cluster composition and quaternary structure of recovered HydA protein sequences based on phylogenetic relationships and the gene contexts of known complete HydA sequences. Numerous recovered HydA are predicted to harbor multiple N- and C-terminal accessory iron-sulfur cluster binding domains and are likely to exist as multisubunit complexes. This study indicates an important role for [FeFe]-hydrogenases in the functioning of the GSL ecosystem and provides new target genes and variants for use in identifying O(2) tolerant enzymes for biotechnological applications. MDPI 2014-11-28 /pmc/articles/PMC4284687/ /pubmed/25464382 http://dx.doi.org/10.3390/ijms151221947 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Boyd, Eric S.
Hamilton, Trinity L.
Swanson, Kevin D.
Howells, Alta E.
Baxter, Bonnie K.
Meuser, Jonathan E.
Posewitz, Matthew C.
Peters, John W.
[FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title_full [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title_fullStr [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title_full_unstemmed [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title_short [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA
title_sort [fefe]-hydrogenase abundance and diversity along a vertical redox gradient in great salt lake, usa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4284687/
https://www.ncbi.nlm.nih.gov/pubmed/25464382
http://dx.doi.org/10.3390/ijms151221947
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