Results 131 to 140 of about 131,481 (151)

Evolution for enhanced extracellular electron transfer in <i>Geobacter sulfurreducens</i> over seventeen years of continuous current generation. [PDF]

Front Microbiol
Holmes DE, Woodard TL, Nevin KP, Vargas M, Romoser K, Holmes SE, Lovley DR.   +6 more
europepmc   +1 more source

Isolation and genomic analysis of "Metallumcola ferriviriculae" MK1, a Gram-positive, Fe(III)-reducing bacterium from the Soudan Underground Mine, an iron-rich Martian analog site. [PDF]

Appl Environ Microbiol
Hsu D, Flynn JR, Schuler CJ, Santelli CM, Toner BM, Bond DR, Gralnick JA.   +6 more
europepmc   +1 more source

Metagenomic insights into microbial communities of terrestrial mud volcanos: functional diversity of subsurface archaea and bacteria. [PDF]

Front Microbiol
Kadnikov VV, Mardanov AV, Beletsky AV, Ravin NV.   +3 more
europepmc   +1 more source

Physiological and transcriptomic response of enriched anammox culture upon elevated hydrazine exposure. [PDF]

Biodegradation
Sari T, Yapsakli K, Akgul D, Mertoglu B.
europepmc   +1 more source

Determinants of Multiheme Cytochrome Extracellular Electron Transfer Uncovered by Systematic Peptide Insertion

Biochemistry, 2022
The multiheme cytochrome MtrA enables microbial respiration by transferring electrons across the outer membrane to extracellular electron acceptors. While structural studies have identified residues that mediate the binding of MtrA to hemes and to other ...
Jonathan J Silberg, Lin Su, Caroline M Ajo-Franklin   +2 more
exaly   +3 more sources

Ultrafast Light-Driven Electron Transfer in a Ru(II)tris(bipyridine)-Labeled Multiheme Cytochrome

Journal of the American Chemical Society, 2019
Multiheme cytochromes attract much attention for their electron transport properties. These proteins conduct electrons across bacterial cell walls and along extracellular filaments and when purified can serve as bionanoelectronic junctions.
Stephen R. Meech, Nicholas Watmough, Xiuyun Jiang   +2 more
exaly   +3 more sources

Crystal structure of a dimeric octaheme cytochrome c3 (Mr 26000) from Desulfovibrio desulfuricans Norway

Structure, 1996
International audienceBACKGROUND: The octaheme cytochrome C3 (M(r) 26,000; cc3) from Desulfovibrio desulfuricans Norway is a dimeric cytochrome made up of two identical subunits, each containing four heme groups.
R Haser, F Guerlesquin, M Czjzek
exaly   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Interfacing the enzyme multiheme cytochrome nitrite reductase with pencil lead electrodes: Towards a disposable biosensor for cyanide surveillance in the environment

Biosensors and Bioelectronics, 2021
Ana S Viana, Tiago Monteiro
exaly  

Heterologous expression and purification of a multiheme cytochrome from a Gram-positive bacterium capable of performing extracellular respiration

Protein Expression and Purification, 2015
Catarina M Paquete, Ricardo O Louro
exaly