ArticleBiotechnology for biofuels2013
Conversion of fatty aldehydes into alk (a/e)nes by in vitro reconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system.
Article in Biotechnology for biofuels, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 59 citations in OpenAlex.
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- The Prokaryotic MicroalgaPolish journal of microbiology · 2023Article
- Recent advances in the improvement of cyanobacterial enzymes for bioalkane production.Microbial cell factories · 2022Review
- Insights into cyanobacterial alkane biosynthesis.Journal of industrial microbiology & biotechnology · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- A novel C-terminal degron identified in bacterial aldehyde decarbonylases using directed evolution.Biotechnology for biofuels · 2020Article
- Continuous photoproduction of hydrocarbon drop-in fuel by microbial cell factories.Scientific reports · 2019Article
- A force awakens: exploiting solar energy beyond photosynthesis.Journal of experimental botany · 2019Review
- Identification of non-conserved residues essential for improving the hydrocarbon-producing activity of cyanobacterial aldehyde-deformylating oxygenase.Biotechnology for biofuels · 2019Article
- Drop-in biofuel production using fatty acid photodecarboxylase fromBiotechnology for biofuels · 2019Article
- A consensus-guided approach yields a heat-stable alkane-producing enzyme and identifies residues promoting thermostability.The Journal of biological chemistry · 2018Article
- Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins.Photosynthesis research · 2017Review
- Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship.BMC biotechnology · 2017Article
- In vitro reconstitution of the cyclosporine specific P450 hydroxylases using heterologous redox partner proteins.Journal of industrial microbiology & biotechnology · 2017Article
- Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase.Biotechnology for biofuels · 2016Article
- Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length.Biotechnology for biofuels · 2016Article
- Reconstitution of the In Vitro Activity of the Cyclosporine-Specific P450 Hydroxylase from Sebekia benihana and Development of a Heterologous Whole-Cell Biotransformation System.Applied and environmental microbiology · 2015Article
- A microbial platform for renewable propane synthesis based on a fermentative butanol pathway.Biotechnology for biofuels · 2015Article
- Heterogeneity of alkane chain length in freshwater and marine cyanobacteria.Frontiers in bioengineering and biotechnology · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBiosynthesis of fatty alk(a/e)ne in cyanobacteria has been considered as a potential basis for the sunlight-driven and carbon-neutral bioprocess producing advanced solar biofuels. Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in that pathway. The heterologous or chemical reducing systems were generally used in in vitro ADO activity assay. The cognate electron transfer system from cyanobacteria to support ADO activity is still unknown.
resultsWe identified the potential endogenous reducing system including ferredoxin (Fd) and ferredoxin-NADP+ reductase (FNR) to support ADO activity in Synechococcus elongatus PCC7942. ADO (Synpcc7942_1593), FNR (SynPcc7942_0978), and Fd (SynPcc7942_1499) from PCC7942 were cloned, overexpressed, purified, and characterized. ADO activity was successfully supported with the endogenous electron transfer system, which worked more effectively than the heterologous and chemical ones. The results of the hybrid Fd/FNR reducing systems demonstrated that ADO was selective against Fd. And it was observed that the cognate reducing system produced less H2O2 than the heterologous one by 33% during ADO-catalyzed reactions. Importantly, kcat value of ADO 1593 using the homologous Fd/FNR electron transfer system is 3.7-fold higher than the chemical one.
conclusionsThe cognate electron transfer system from cyanobacteria to support ADO activity was identified and characterized. For the first time, ADO was functionally in vitro reconstituted with the endogenous reducing system from cyanobacteria, which supported greater activity than the surrogate and chemical ones, and produced less H2O2 than the heterologous one. The identified Fd/FNR electron transfer system will be potentially useful for improving ADO activity and further enhancing the biosynthetic efficiency of hydrocarbon biofuels in cyanobacteria.
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