Interaction of cytochrome c and its precursor apocytochrome c with various phospholipids
نویسندگان
چکیده
منابع مشابه
Apocytochrome c
The cytochrome c import pathway differs markedly from the general route taken by the majority of other imported proteins, which is characterized by the import involvement of namely, surface receptors, the general insertion protein (GIP), contact sites and by the requirement of a membrane potential (AO). Unique features of both the cytoehrome c precursor (apocytoehrome c) and of the mechanism th...
متن کاملAssembly of cytochrome c. Apocytochrome c is bound to specific sites on mitochondria before its conversion to holocytochrome c.
Transport of apocytochrome c across the outer mitochondrial membrane and conversion to holocytochrome c were studied in vitro. Apocytochrome c was synthesized in a cell-free homogenate from Neurosporu crussu. Transfer in vitro was accomplished in a reconstituted system consisting of the postribosomal supernatant of the cell-free homogenate and of isolated and purified mitochondria from Neurospo...
متن کاملThermotropic behavior of dimyristoylphosphatidylglycerol and its interaction with cytochrome c.
The thermotropic behavior of dimyristoylphosphatidylglycerol (DMPG) in the absence and presence of cytochrome c under low-salt conditions has been investigated using differential scanning calorimetry (DSC), 31P nuclear magnetic resonance (31P NMR), electron spin resonance (ESR), viscosity, light scattering, and electron microscopy. In the absence of protein, the lipid undergoes a sequence of tr...
متن کاملSpecificity of the interaction of amino- and carboxy-terminal fragments of the mitochondrial precursor protein apocytochrome c with negatively charged phospholipids. A spin-label electron spin resonance study.
The contribution of the various regions of the mitochondrial precursor protein apocytochrome c to the interaction of the protein with phosphatidylserine dispersions has been studied with chemically and enzymatically prepared fragments of horse heart apocytochrome c and phospholipids spin-labeled at different positions of the sn-2 chain. Three amino-terminal heme-less peptides, two heme-containi...
متن کاملSpectroscopic studies on the conformation of cytochrome c and apocytochrome c.
The appearance of the downfield region of the PMR spectrum of apocytochrome c is consistent with that of an extensively disordered protein. The resonances of the three histidine C-2 protons are almost equivalent and have a pKa of 6.2. In contrast, this region of the ferricytochrome c PMR spectrum shows many sharp resonances, due to the tertiary structure of the protein and contact shifts from t...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1983
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1983.tb01520.x