{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Vamshi Krishna K"],"pubmed_abstract":["In microbial electrochemical systems, transport of electrons from bacteria to an electrode is the key to its functioning. However, the roles of several electron transport proteins, especially the membrane-bound dehydrogenases which link cellular metabolism to EET pathway are yet to be identified. NDH-2 is a non-proton pumping NADH dehydrogenase located in the inner membrane of several bacteria like <i>Bacillus subtilis</i>, <i>Escherichia coli</i>, etc. Unlike NADH dehydrogenase I, NDH-2 is not impeded by a high proton motive force thus helping in the increase of metabolic flux and carbon utilization. In the current study, NADH dehydrogenase II protein (NDH-2) was heterologously expressed from <i>B. subtilis</i> into <i>E. coli</i> BL21 (DE3) for enhancing electron flux through EET pathway"],"journal":["Frontiers in microbiology"],"pagination":["880"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6513898"],"repository":["biostudies-literature"],"pubmed_title":["Purification and Characterization of NDH-2 Protein and Elucidating Its Role in Extracellular Electron Transport and Bioelectrogenic Activity."],"pmcid":["PMC6513898"],"pubmed_authors":["Vamshi Krishna K","Venkata Mohan S"],"additional_accession":[]},"is_claimable":false,"name":"Purification and Characterization of NDH-2 Protein and Elucidating Its Role in Extracellular Electron Transport and Bioelectrogenic Activity.","description":"In microbial electrochemical systems, transport of electrons from bacteria to an electrode is the key to its functioning. However, the roles of several electron transport proteins, especially the membrane-bound dehydrogenases which link cellular metabolism to EET pathway are yet to be identified. NDH-2 is a non-proton pumping NADH dehydrogenase located in the inner membrane of several bacteria like <i>Bacillus subtilis</i>, <i>Escherichia coli</i>, etc. Unlike NADH dehydrogenase I, NDH-2 is not impeded by a high proton motive force thus helping in the increase of metabolic flux and carbon utilization. In the current study, NADH dehydrogenase II protein (NDH-2) was heterologously expressed from <i>B. subtilis</i> into <i>E. coli</i> BL21 (DE3) for enhancing electron flux through EET pathway","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2026-04-08T05:34:36.512Z","creation":"2019-06-06T23:14:18Z"},"accession":"S-EPMC6513898","cross_references":{"pubmed":["31133996"],"doi":["10.3389/fmicb.2019.00880"]}}