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• W2169369169 abstract "Cyanobacteria use sunlight and water to produce hydrogen gas (H₂), which is potentially useful as a clean and renewable biofuel. Photobiological H₂ arises primarily as an inevitable by-product of N₂ fixation by nitrogenase, an oxygen-labile enzyme typically containing an iron-molybdenum cofactor (FeMo-co) active site. In Anabaena sp. strain 7120, the enzyme is localized to the microaerobic environment of heterocysts, a highly differentiated subset of the filamentous cells. In an effort to increase H₂ production by this strain, six nitrogenase amino acid residues predicted to reside within 5 Å of the FeMo-co were mutated in an attempt to direct electron flow selectively toward proton reduction in the presence of N₂. Most of the 49 variants examined were deficient in N₂-fixing growth and exhibited decreases in their in vivo rates of acetylene reduction. Of greater interest, several variants examined under an N₂ atmosphere significantly increased their in vivo rates of H₂ production, approximating rates equivalent to those under an Ar atmosphere, and accumulated high levels of H₂ compared to the reference strains. These results demonstrate the feasibility of engineering cyanobacterial strains for enhanced photobiological production of H₂ in an aerobic, nitrogen-containing environment." @default.
• W2169369169 created "2016-06-24" @default.
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• W2169369169 date "2010-10-15" @default.
• W2169369169 modified "2023-09-23" @default.
• W2169369169 title "Site-Directed Mutagenesis of the <i>Anabaena</i> sp. Strain PCC 7120 Nitrogenase Active Site To Increase Photobiological Hydrogen Production" @default.
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• W2169369169 doi "https://doi.org/10.1128/aem.01056-10" @default.
• W2169369169 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2953041" @default.
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