Next Article in Journal
Gypenosides Protected the Neural Stem Cells in the Subventricular Zone of Neonatal Rats that Were Prenatally Exposed to Ethanol
Next Article in Special Issue
Designed Surface Residue Substitutions in [NiFe] Hydrogenase that Improve Electron Transfer Characteristics
Previous Article in Journal
Role of Aeromonas hydrophila Flagella Glycosylation in Adhesion to Hep-2 Cells, Biofilm Formation and Immune Stimulation
Previous Article in Special Issue
Advances in the Function and Regulation of Hydrogenase in the Cyanobacterium Synechocystis PCC6803
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2014, 15(12), 21947-21966; doi:10.3390/ijms151221947

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

1
Department of Microbiology and Immunology, Montana State University, Bozeman, MT 59717, USA
2
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA
3
Department of Biology and the Great Salt Lake Institute, Westminster College, Salt Lake City, UT 84105, USA
4
Department of Chemistry and Geochemistry, Colorado School of Mines, Golden, CO 80401, USA
*
Author to whom correspondence should be addressed.
Received: 21 October 2014 / Revised: 11 November 2014 / Accepted: 13 November 2014 / Published: 28 November 2014
(This article belongs to the Special Issue Photosynthesis and Biological Hydrogen Production)
View Full-Text   |   Download PDF [2721 KB, uploaded 28 November 2014]   |  

Abstract

The use of [FeFe]-hydrogenase enzymes for the biotechnological production of H2 or other reduced products has been limited by their sensitivity to oxygen (O2). Here, we apply a PCR-directed approach to determine the distribution, abundance, and diversity of hydA gene fragments along co-varying salinity and O2 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 O2 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 H2 transfer and O2 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 O2 tolerant enzymes for biotechnological applications. View Full-Text
Keywords: [FeFe]-hydrogenase; electron bifurcation; hydrogen; photosynthesis; fermentation; oxygen tolerance; hydropathy; hypersaline [FeFe]-hydrogenase; electron bifurcation; hydrogen; photosynthesis; fermentation; oxygen tolerance; hydropathy; hypersaline
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Boyd, E.S.; Hamilton, T.L.; Swanson, K.D.; Howells, A.E.; Baxter, B.K.; Meuser, J.E.; Posewitz, M.C.; Peters, J.W. [FeFe]-Hydrogenase Abundance and Diversity along a Vertical Redox Gradient in Great Salt Lake, USA. Int. J. Mol. Sci. 2014, 15, 21947-21966.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top