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Title: Development of a Rhodobacter capsulatus self-reporting model system for optimizing light-dependent, [FeFe]-hydrogenase-driven H 2 production

Abstract

The photosynthetic bacterium Rhodobacter capsulatus normally photoproduces H 2 as a by-product of its nitrogenase-catalyzed nitrogen-fixing activity. Such H 2 production, however, is expensive from a metabolic perspective, requiring nearly four times as many photons as the equivalent algal hydrogenase-based system. Here we report the insertion of a Clostridium acetobutylicum [FeFe]-hydrogenase and its three attendant hydrogenase assembly proteins into an R. capsulatus strain lacking its native uptake hydrogenase. Further, this strain is modified to fluoresce upon sensing H 2. The resulting strain photoproduces H 2 and self-reports its own H 2 production through fluorescence. Furthermore, this model system represents a unique method of developing hydrogenase-based H 2 production in R. capsulatus, may serve as a powerful system for in vivo directed evolution of hydrogenases and hydrogenase-associated genes, and provides a means of screening for increased metabolic production of H 2.

Authors:
 [1];  [2];  [2];  [3]
  1. GeneBiologics, LLC, Boulder, CO (United States)
  2. United States Air Force Academy, Colorado Springs, CO (United States)
  3. National Renewable Energy Lab. (NREL), Golden, CO (United States)
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1339249
Report Number(s):
NREL/JA-2700-66611
Journal ID: ISSN 0006-3592
Grant/Contract Number:
AC36-08GO28308; AC36-08GC28308z
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biotechnology and Bioengineering
Additional Journal Information:
Journal Volume: 114; Journal Issue: 2; Journal ID: ISSN 0006-3592
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; R. capsulatus H2 sensor; high-throughput screening; photobiohydrogen; nitrogenase; H2 production

Citation Formats

Wecker, Matt S. A., Beaton, Stephen E., Chado, Robert A., and Ghirardi, Maria L.. Development of a Rhodobacter capsulatus self-reporting model system for optimizing light-dependent, [FeFe]-hydrogenase-driven H2 production. United States: N. p., 2016. Web. doi:10.1002/bit.26076.
Wecker, Matt S. A., Beaton, Stephen E., Chado, Robert A., & Ghirardi, Maria L.. Development of a Rhodobacter capsulatus self-reporting model system for optimizing light-dependent, [FeFe]-hydrogenase-driven H2 production. United States. doi:10.1002/bit.26076.
Wecker, Matt S. A., Beaton, Stephen E., Chado, Robert A., and Ghirardi, Maria L.. 2016. "Development of a Rhodobacter capsulatus self-reporting model system for optimizing light-dependent, [FeFe]-hydrogenase-driven H2 production". United States. doi:10.1002/bit.26076. https://www.osti.gov/servlets/purl/1339249.
@article{osti_1339249,
title = {Development of a Rhodobacter capsulatus self-reporting model system for optimizing light-dependent, [FeFe]-hydrogenase-driven H2 production},
author = {Wecker, Matt S. A. and Beaton, Stephen E. and Chado, Robert A. and Ghirardi, Maria L.},
abstractNote = {The photosynthetic bacterium Rhodobacter capsulatus normally photoproduces H2 as a by-product of its nitrogenase-catalyzed nitrogen-fixing activity. Such H2 production, however, is expensive from a metabolic perspective, requiring nearly four times as many photons as the equivalent algal hydrogenase-based system. Here we report the insertion of a Clostridium acetobutylicum [FeFe]-hydrogenase and its three attendant hydrogenase assembly proteins into an R. capsulatus strain lacking its native uptake hydrogenase. Further, this strain is modified to fluoresce upon sensing H2. The resulting strain photoproduces H2 and self-reports its own H2 production through fluorescence. Furthermore, this model system represents a unique method of developing hydrogenase-based H2 production in R. capsulatus, may serve as a powerful system for in vivo directed evolution of hydrogenases and hydrogenase-associated genes, and provides a means of screening for increased metabolic production of H2.},
doi = {10.1002/bit.26076},
journal = {Biotechnology and Bioengineering},
number = 2,
volume = 114,
place = {United States},
year = 2016,
month = 8
}

Journal Article:
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