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Evidence for Quinol Oxidation Activity of ImoA, a Novel NapC/NirT Family Protein from the Neutrophilic Fe(II)-Oxidizing Bacterium Sideroxydans lithotrophicus ES-1

Abhiney Jain, Anaísa Coelho, Joana Madjarov, Catarina M. Paquete, Jeffrey A. Gralnick

2022mBio18 citationsDOIOpen Access PDF

Abstract

Fe(II)-oxidizing bacteria play an important role in biogeochemical cycles. At circumneutral pH, these organisms perform extracellular electron transfer, taking up electrons from Fe(II) outside the cell, potentially through a porin-cytochrome complex in the outer membrane encoded by the Mto pathway.

Topics & Concepts

Shewanella oneidensisPeriplasmic spacePorinBacterial outer membraneCytochromeChemistryElectron transferElectron transport chainBiochemistryShewanellaBiophysicsBiologyBacteriaEscherichia coliGeneticsEnzymePhotochemistryGeneMicrobial Fuel Cells and BioremediationMetal Extraction and BioleachingRadioactive element chemistry and processing
Evidence for Quinol Oxidation Activity of ImoA, a Novel NapC/NirT Family Protein from the Neutrophilic Fe(II)-Oxidizing Bacterium Sideroxydans lithotrophicus ES-1 | Litcius