S13.7 Heterologous overexpression of eukaryotic cytochrome c and cytochrome c heme lyase to study the mechanism of cytochrome c maturation
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چکیده
منابع مشابه
Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria.
The import of cytochrome c into Neurospora crassa mitochondria was examined at distinct stages in vitro. The precursor protein, apocytochrome c, binds to mitochondria with high affinity and specificity but is not transported completely across the outer membrane in the absence of conversion to holocytochrome c. The bound apocytochrome c is accessible to externally added proteases but at the same...
متن کاملCytochrome c heme lyase activity of yeast mitochondria.
A highly efficient in vitro system was established for measuring by high performance liquid chromatography the formation of holocytochrome c by yeast mitochondria. Holocytochrome c formation required reducing agents, of which dithiothreitol was the most effective. With biosynthetically made, pure Drosophila melanogaster apocytochrome c and Saccharomyces cerevisiae mitochondria, the activity of ...
متن کاملCytochrome c heme lyase can mature a fusion peptide composed of the amino-terminal residues of horse cytochrome c.
It is shown that cytochrome c heme lyase (CCHL) attaches heme covalently to peptides composed of the N-terminal segment of cyt c fused to a non-heme containing protein, lending insight into the substrate specificity of CCHL and providing a new route to artificial heme proteins.
متن کاملA mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria.
The nuclear cyt-2-1 mutant of Neurospora crassa is characterized by a gross deficiency of cytochrome c (Bertrand, H., and Collins, R. A. (1978) Mol. Gen. Genet. 166, 1-13). The mutant produces mRNA that can be translated into apocytochrome c in vitro. Apocytochrome c is also synthesized in vivo in cyt-2-1, but it is rapidly degraded and thus does not accumulate in the cytosol. Mitochondria from...
متن کاملHeme A of Cytochrome c Oxidase
Heme A, isolated from bovine heart muscle by procedures which include extractions into pyridine/ chloroform and two-phase, liquid-liquid chromatography on Celite, has been converted to several derivatives. Examination of the proton nuclear magnetic resonance (PMR) spectra and other properties of these derivatives reveals heme A to be the iron complex of %formyl-6,7-bis(2”-hydroxycarbonylethyl)-...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2008
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2008.05.351