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Metabolic Adaptations in a H-2 Producing Heterocyst-Forming Cyanobacterium : Potentials and Implications for Biological Engineering

Ekman, Martin (författare)
Uppsala universitet,Mikrobiell kemi
Ow, Saw Yen (författare)
ChELSI Institute, Department of Chemical and Process Engineering, The University of Sheffield
Holmqvist, Marie (författare)
Uppsala universitet,Mikrobiell kemi
visa fler...
Zhang, Xiaohui (författare)
Uppsala universitet,Mikrobiell kemi
van Wagenen, Jon (författare)
Uppsala universitet,Mikrobiell kemi
Wright, Phillip C. (författare)
ChELSI Institute, Department of Chemical and Process Engineering, The University of Sheffield
Stensjö, Karin (författare)
Uppsala universitet,Mikrobiell kemi
visa färre...
 (creator_code:org_t)
American Chemical Society (ACS), 2011
2011
Engelska.
Ingår i: Journal of Proteome Research. - : American Chemical Society (ACS). - 1535-3893 .- 1535-3907. ; 10:4, s. 1772-1784
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Nostoc punctiforme ATCC 29133 is a photoautotrophic cyanobacterium with the ability to fix atmospheric nitrogen and photoproduce hydrogen through the enzyme nitrogenase. The H-2 produced is reoxidized by an uptake hydrogenase. Inactivation of the uptake hydrogenase in N. punctiforme leads to increased H-2 release but unchanged rates of N-2 fixation, indicating redirected metabolism. System-wide understanding of the mechanisms of this metabolic redirection was obtained using complementary quantitative proteomic approaches, at both the filament and the heterocyst level. Of the total 1070 identified and quantified proteins, 239 were differentially expressed in the uptake hydrogenase mutant (NHM5) as compared to wild type. Our results indicate that the inactivation of uptake hydrogenase in N. punctiforme changes the overall metabolic equilibrium, affecting both oxygen reduction mechanisms in hetcrocysts as well as processes providing reducing equivalents for metabolic functions such as N-2 fixation. We identify specific metabolic processes used by NHM5 to maintain a high rate of N-2 fixation, and thereby potential targets for further improvement of nitrogenase based H-2 photogeneration. These targets include, but are not limited to, components of the oxygen scavenging capacity and cell envelope of heterocysts and proteins directly or indirectly involved in reduced carbon transport from vegetative cells to heterocysts.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

iTRAQ
shotgun proteomics
Nostoc punctiforme ATCC 29133
uptake hydrogenase mutant
nitrogenase
dinitrogen fixation
heterocysts
NHMS
biotechnology
Molecular biology
Molekylärbiologi

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