Results 21 to 30 of about 19,718,861 (281)

Multi-heme cytochrome-mediated extracellular electron transfer by the anaerobic methanotroph ‘Candidatus Methanoperedens nitroreducens’

open access: yesNature Communications, 2023
Anaerobic methanotrophic archaea (ANME) carry out anaerobic oxidation of methane, thus playing a crucial role in the methane cycle. Previous genomic evidence indicates that multi-heme c-type cytochromes (MHCs) may facilitate the extracellular electron ...
Xueqin Zhang   +9 more
doaj   +1 more source

New insight into the mechanism of mitochondrial cytochrome c function. [PDF]

open access: yesPLoS ONE, 2017
We investigate functional role of the P76GTKMIFA83 fragment of the primary structure of cytochrome c. Based on the data obtained by the analysis of informational structure (ANIS), we propose a model of functioning of cytochrome c. According to this model,
Rita V Chertkova   +9 more
doaj   +1 more source

Different outer membrane c‐type cytochromes are involved in direct interspecies electron transfer to Geobacter or Methanosarcina species

open access: yesmLife, 2022
Direct interspecies electron transfer (DIET) may be most important in methanogenic environments, but mechanistic studies of DIET to date have primarily focused on cocultures in which fumarate was the terminal electron acceptor.
Dawn E. Holmes   +5 more
doaj   +1 more source

Reduction Kinetic of Water Soluble Metal Salts by Geobacter sulfurreducens: Fe2+/Hemes Stabilize and Regulate Electron Flux Rates

open access: yesFrontiers in Microbiology, 2022
Geobacter sulfurreducens is a widely applied microorganism for the reduction of toxic metal salts, as an electron source for bioelectrochemical devices, and as a reagent for the synthesis of nanoparticles.
Maksym Karamash   +6 more
doaj   +1 more source

Cytochrome c and superoxide [PDF]

open access: yesJBIC Journal of Biological Inorganic Chemistry, 2013
Wegerich et al. (J. Biol. Inorg. Chem. 18:429-440, 2013), working with singly modified human cytochromes c, claim to have found a new mechanism for the reduction of iron(III) cytochrome c by superoxide. I show that electron transfer by way of the solvent-accessible haem edge - a mechanism not considered by Wegerich et al.
openaire   +4 more sources

The electron transport chains of Neisseria meningitidis [PDF]

open access: yes, 2007
Neisseria meningitidis contains c-type and b-type cytochromes. Oxidation of c-type and b-type cytochromes by oxygen was observed in both cells grown under aerobic and denitrifying conditions, whereas oxidation of cytochromes by nitrite was only seen in ...
Deeudom, Manu
core   +5 more sources

STRUCTURAL BASIS FOR REDOX POTENTIAL DIFFERENCES OF C-TYPE CYTOCHROMES.

open access: yes, 1982
STRUCTURAL BASIS FOR REDOX POTENTIAL DIFFERENCES OF C-TYPE ...
GEORGE G. SCHLAUDER (7975631)
core   +4 more sources

Electrochemical Characterization of the Periplasmic PpcA c‐Cytochrome of Geobacter sulfurreducens Reveals Its Affinity for Uranium

open access: yesChemElectroChem, 2023
Geobacter bacteria produce conductive pili appendages and an outer membrane‐anchored lipopolysaccharide to immobilize uranium extracellularly. Yet, some radionuclide enters the cell envelope, where is rapidly mineralized by periplasmic c‐cytochromes.
Dr. Bhushan P. Awate   +2 more
doaj   +1 more source

Real-time measurements of the redox states of c-type cytochromes in electroactive biofilms: a confocal resonance Raman Microscopy study.

open access: yesPLoS ONE, 2014
Confocal Resonance Raman Microscopy (CRRM) was used to probe variations of redox state of c-type cytochromes embedded in living mixed-culture electroactive biofilms exposed to different electrode polarizations, under potentiostatic and potentiodynamic ...
Bernardino Virdis   +3 more
doaj   +1 more source

Import of cytochrome c into mitochondria. Cytochrome c heme lyase [PDF]

open access: yesEuropean Journal of Biochemistry, 1987
The import of cytochrome c into mitochondria can be resolved into a number of discrete steps. Here we report on the covalent attachment of heme to apocytochrome c by the enzyme cytochrome c heme lyase in mitochondria from Neurospora crassa. A new method was developed to measure directly the linkage of heme to apocytochrome c. This method is independent
D W, Nicholson, H, Köhler, W, Neupert
openaire   +2 more sources

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