Results 51 to 60 of about 146,105 (308)

Coordination of metal center biogenesis in human cytochrome c oxidase

open access: yesNature Communications, 2022
Mitochondrial cytochrome c oxidase is a heme aa3-copper oxygen reductase. Here, authors report that metal center-specific metallochaperones form dynamic assemblies to control heme a biosynthesis and coordinate copper transfer to the copper sites.
Eva Nývltová   +4 more
doaj   +1 more source

Inactivation of Cytochrome-c with Glucose Oxidase

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2004
A novel reaction of cytochrome-c from the horse heart with the enzyme glucose oxidase from Aspergillus niger (EC 1.1.3.4), in acidic media is described. Glucose oxidase is able to induce a rapid, profound and irreversible physico-chemical change in cytochrome-c, under anaerobic conditions and in the presence of glucose.
Leskovac, Vladimir   +3 more
openaire   +2 more sources

Electron transfer between complexes III and IV in S. cerevisiae mitochondrial membranes

open access: yesFEBS Letters, EarlyView.
Mitochondrial oxidative phosphorylation in S. cerevisiae mitoplasts is limited by complex IV catalytic capacity, rather than two‐dimensional cytochrome c diffusion. At physiological cytochrome c : supercomplex ratios at salinity equivalent to that of 20 mm monovalent salt, activity is maximized, indicating that this low ionic strength accurately mimics
Ana Paula Lobez   +2 more
wiley   +1 more source

MITRAC7 Acts as a COX1-Specific Chaperone and Reveals a Checkpoint during Cytochrome c Oxidase Assembly

open access: yesCell Reports, 2015
Cytochrome c oxidase, the terminal enzyme of the respiratory chain, is assembled from mitochondria- and nuclear-encoded subunits. The MITRAC complex represents the central assembly intermediate during this process as it receives imported subunits and ...
Sven Dennerlein   +8 more
doaj   +1 more source

The respiratory arsenite oxidase: structure and the role of residues surrounding the Rieske cluster [PDF]

open access: yes, 2013
The arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate.
Muse Oke (452182)   +56 more
core   +1 more source

Proteasomal degradation of intracellularly expressed Amblyomin‐X limits suicide gene therapy potential in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel   +4 more
wiley   +1 more source

Differentiation and cell density upregulate cytochrome c levels in megakaryoblastic cell lines: Implications for analysis of CYCS-associated thrombocytopenia. [PDF]

open access: yesPLoS ONE, 2017
Mutations in the cytochrome c gene (CYCS) cause autosomal dominant thrombocytopenia by an unknown mechanism. While attempting to generate megakaryoblastic cell lines exogenously expressing cytochrome c variants, we discovered that endogenous cytochrome c
Lily Ong   +2 more
doaj   +1 more source

Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo.

open access: yes, 2008
The cytochrome bd-I complex of Escherichia coli is a respiratory terminal oxidase and an integral component of the cytoplasmic membrane. As with other respiratory components, the organization and dynamics of this complex in living membranes is unknown ...
Mullineaux, CW   +3 more
core   +1 more source

The dinuclear Cuᴀ centre of cytochrome oxidase

open access: yes, 2021
Cytochrome c oxidase is the last enzyme in mitochondrial and many bacterial respiratory chains. It catalyzes electron transfer from cytochrome c to molecular oxygen and transfers free energy of this reaction into a transmembrane proton electrochemical ...
Lappalainen, Pekka
core   +1 more source

Time‐restricted feeding prior to Mycobacterium tuberculosis infection reduces tissue CD4+ T cells with limited impact on bacterial clearance

open access: yesFEBS Open Bio, EarlyView.
Time‐restricted feeding (TRF) in mice increased liver fatty acid oxidation and decreased fatty acid biosynthesis. These alterations persisted when TRF was discontinued and the host was infected with Mycobacterium tuberculosis. Pre‐exposure to TRF did not alter tissue (lung and spleen) mycobacterial burden but significantly reduced CD3+ T cells in lungs
Ashish Gupta   +7 more
wiley   +1 more source

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