Results 21 to 30 of about 19,855,151 (220)
Biogenesis of Cytochrome c in Neurospora crassa [PDF]
# 1. Precipitating antibodies specific for apocytochrome c and holocytochrome c, respectively, were employed to study synthesis and intracellular transport of cytochrome c in Neurospora in vitro. # 2.
Korb, Harald, Neupert, Walter
openaire +3 more sources
HEME Trafficking by the Cytochrome C Biogenesis Pathways [PDF]
Cytochromes function in electron transport chains to perform critical cellular functions, such as respiration and photosynthesis. Cytochromes c are unique due to their requirement for the covalent attachment of heme via two thioether bonds at a conserved CXXCH motif. Three pathways have been identified for cytochrome c maturation: System I (prokaryotes)
Molly C. Sutherland +2 more
openaire +2 more sources
Mitochondrial cytochrome c biogenesis: no longer an enigma [PDF]
Cytochromes c (cyt c) and c1 are heme proteins that are essential for aerobic respiration. Release of cyt c from mitochondria is an important signal in apoptosis initiation. Biogenesis of c-type cytochromes involves covalent attachment of heme to two cysteines (at a conserved CXXCH sequence) in the apocytochrome.
Shalon E, Babbitt +4 more
openaire +2 more sources
Continued surprises in the cytochrome c biogenesis story [PDF]
Cytochromes c covalently bind their heme prosthetic groups through thioether bonds between the vinyl groups of the heme and the thiols of a CXXCH motif within the protein. In Gram-negative bacteria, this process is catalyzed by the Ccm (cytochrome c maturation) proteins, also called System I.
Sawyer, Elizabeth B, Barker, Paul D
openaire +2 more sources
Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome
Although intracellular heme trafficking must occur for heme protein assembly, only a few heme transporters have been unequivocally discovered and nothing is known about their structure or mechanisms.
Molly C. Sutherland +5 more
doaj +1 more source
Biogenesis of mitochondrialc-type cytochromes
Cytochromes c and c1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space; cytochrome c is loosely attached to the surface of the inner mitochondrial membrane, whereas ...
Gonzales, Daniel H., Neupert, Walter
openaire +3 more sources
Yeast cytochrome c oxidase: a model system to study mitochondrial forms of the haem-copper oxidase superfamily. [PDF]
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 +9 more
core +1 more source
Increased liver content of DHA‐derived small lipid autacoids (i.e resolvin D1 and maresin 1) associates with enhanced mitochondrial oxidative phosphorylation, fatty acid β‐oxidation and bioenergetic metabolic flux. These features provide hepatic protection from steatotic, pro‐inflammatory and fibrogenic insults.
Cristina López‐Vicario +12 more
wiley +1 more source
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro +17 more
wiley +1 more source
Biogenesis of eukaryotic cytochrome c oxidase
Eukaryotic cytochrome c oxidase (CcO), the terminal component of the mitochondrial electron transport chain is a heterooligomeric complex that belongs to the superfamily of heme-copper containing terminal oxidases. The enzyme, composed of both mitochondrially and nuclear encoded subunits, is embedded in the inner mitochondrial membrane, where it ...
L, Stiburek +4 more
openaire +2 more sources

