Journal
JOURNAL OF PROTEOME RESEARCH
Volume 10, Issue 4, Pages 1772-1784Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr101055v
Keywords
iTRAQ; shotgun proteomics; Nostoc punctiforme ATCC 29133; uptake hydrogenase mutant; nitrogenase; dinitrogen fixation; heterocysts; NHMS; biotechnology
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Funding
- EU [043340, 212508]
- Swedish Energy Agency
- Knut and Alice Wallenberg Foundation
- Magnus Bergvall Foundation
- EPSRC under the ChELSI Initiative [EP/E036252/1]
- EPSRC [EP/E036252/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/E036252/1] Funding Source: researchfish
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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.
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