Bioelectrochemical reduction of an azo dye by a Shewanella oneidensis MR-1 formed biocathode

Hydrogen metabolism in Shewanella oneidensis MR-1.

Shewanella oneidensis MR-1 is a facultative sediment microorganism which uses diverse compounds, such as oxygen and fumarate, as well as insoluble Fe(III) and Mn(IV) as electron acceptors. The electron donor spectrum is more limited and includes metabolic end products of primary fermenting bacteria, such as lactate, formate, and hydrogen. While the utilization of hydrogen as an electron donor h...

Selenite reduction by Shewanella oneidensis MR-1 is mediated by fumarate reductase in periplasm

In situ reduction of selenite to elemental selenium (Se(0)), by microorganisms in sediments and soils is an important process and greatly affects the environmental distribution and the biological effects of selenium. However, the mechanism behind such a biological process remains unrevealed yet. Here we use Shewanella oneidensis MR-1, a widely-distributed dissimilatory metal-reducing bacterium ...

Molecular underpinnings of Fe(III) oxide reduction by <i>Shewanella oneidensis </i> MR-1

Molecular Underpinnings of Fe(III) Oxide Reduction by Shewanella Oneidensis MR-1

In the absence of O(2) and other electron acceptors, the Gram-negative bacterium Shewanella oneidensis MR-1 can use ferric [Fe(III)] (oxy)(hydr)oxide minerals as the terminal electron acceptors for anaerobic respiration. At circumneutral pH and in the absence of strong complexing ligands, Fe(III) oxides are relatively insoluble and thus are external to the bacterial cells. S. oneidensis MR-1 an...

Characterization of protein-protein interactions involved in iron reduction by Shewanella oneidensis MR-1.

The interaction of proteins implicated in dissimilatory metal reduction by Shewanella oneidensis MR-1 (outer membrane [OM] proteins OmcA, MtrB, and MtrC; OM-associated protein MtrA; periplasmic protein CctA; and cytoplasmic membrane protein CymA) were characterized by protein purification, analytical ultracentrifugation, and cross-linking methods. Five of these proteins are heme proteins, OmcA ...