Results 11 to 20 of about 28,229,161 (299)

Characterization of the key membrane protein cytochrome Cyc2 from Ghiorsea bivora. [PDF]

FEBS Open Bio
This study reports the first detailed biochemical analysis of Cyc2TAG1_1, a cytochrome protein involved in microbial iron oxidation. We produced and purified this enzyme in E. coli, then measured its iron‐oxidizing efficiency, and characterized its electrical and structural properties.
Azizi J, Dolla A, Baymann F, Rommevaux C, Elantak L, Gaussier H, Nouailler M.   +6 more
europepmc   +2 more sources

The Respiratory Chain In Neisseria Species [PDF]

, 2013
This work presents the organization of respiratory chain in Neisseria species. The localization of redox proteins was determined. Lipid-modified azurin (Laz) and nitrite reductase (AniA) are mainly associated with outer membrane.
Li, Xi
core   +5 more sources

Recent insights into the molecular mechanism of ubiquinol oxidation by cytochrome bc₁. [PDF]

FEBS Open Bio
The review reflects on the mechanism of the catalytic reaction in cytochrome bc1: the electron bifurcation that involves the separation of two electrons derived from the quinol oxidation to opposite sides of the enzyme across the membrane. This review summarizes the long‐standing effort to understand the mechanism of quinol oxidation catalyzed by ...
Wójcik-Augustyn A, Osyczka A, Sarewicz M.   +2 more
europepmc   +2 more sources

Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging

Frontiers in Cell and Developmental Biology, 2022
The normal functioning of sperm cells requires cytochrome c in the redox balanced forms: reduced and oxidized. The oxidized form of cytochrome c is localized in the mitochondrial intermembrane space and is a part of the electron transport chain.
Halina Abramczyk, Bogna Sobkiewicz, Renata Walczak-Jędrzejowska, Katarzyna Marchlewska, Jakub Surmacki   +4 more
doaj   +1 more source

NMR Study on the Mechanism of Cytochrome c Methionine Oxidation

Chinese Journal of Magnetic Resonance, 2023
Mitochondria generate reactive oxygen species (ROS) during respiration. Low levels of ROS are conducive to signal transduction, whereas excessive accumulation of ROS can lead to protein oxidative modification.
ZHAO Beibei, ZHAN Jianhua, HU Qin, ZHU Qinjun, LIU Maili, ZHANG Xu   +5 more
doaj   +1 more source

Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c‐type cytochromes [PDF]

Molecular Microbiology, 2006
SummaryIn all organisms, haem is post‐translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c‐type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem–apocytochrome ligation per se.
Serdar, Turkarslan, Carsten, Sanders, Fevzi, Daldal   +2 more
openaire   +2 more sources

Hypericin Enhances Paclitaxel-Induced B16-F10 Cell Apoptosis by Activating a Cytochrome c Release–Dependent Pathway

Frontiers in Pharmacology, 2021
The enhanced inhibitory effect of paclitaxel (PTX) combined with hypericin (HY) on B16-F10 cells may be realized through the ROS-related cytochrome c release pathway.
Liyun Sun, Zixuan Li, Huoli Shang, Xiujuan Xin   +3 more
doaj   +1 more source

Heme-a, the heme prosthetic group of cytochrome c oxidase, is increased in Alzheimer's disease [PDF]

Neuroscience Letters, 2009
Heme-a, is the heme prosthetic group of cytochrome c oxidase (COX), the terminal complex of the mitochondrial electron transport chain. We measured heme-a levels in postmortem brain tissue from nine patients diagnosed with dementia: Alzheimer's disease (AD) was the primary diagnosis in five, AD/diffuse Lewy body disease (DLBD) was diagnosed in two ...
Barney E, Dwyer, Meghan L, Stone, Nadia, Gorman, Peter R, Sinclair, George, Perry, Mark A, Smith, Xiongwei, Zhu   +6 more
openaire   +2 more sources

Yeast cytochrome c oxidase: a model system to study mitochondrial forms of the haem-copper oxidase superfamily. [PDF]

, 2012
The known subunits of yeast mitochondrial cytochrome c oxidase are reviewed. The structures of all eleven of its subunits are explored by building homology models based on the published structures of the homologous bovine subunits and similarities and ...
Maréchal, A, Amandine Maréchal, Peter R. Rich, Brigitte Meunier, Lee, D, Orengo, C, Meunier, B, Christine Orengo, David Lee, Rich, PR   +9 more
core   +1 more source

Unfolded States of Heme Proteins [PDF]

, 2010
Cytochromes adopt discrete structures when the heme cofactor is present. Since the heme provides crucial contacts in the native protein, this hydrophobic prosthetic group plays an important role in the folding mechanism and introduces interesting ...
Pribisko Yen, Melanie Anne
core   +1 more source