Heme Protein Engineering of Cytochrome <i>b</i>-562
نویسندگان
چکیده
منابع مشابه
Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase.
Heme oxygenase (HO) catalyzes the rate-limiting step in the O2-dependent degradation of heme to biliverdin, CO, and iron with electrons delivered from NADPH via cytochrome P450 reductase (CPR). Biliverdin reductase (BVR) then catalyzes conversion of biliverdin to bilirubin. We describe mutagenesis combined with kinetic, spectroscopic (fluorescence and NMR), surface plasmon resonance, cross-link...
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The active site of cytochrome c (Cyt c) consists of a heme covalently linked to a pentapeptide segment (Cys-X-X-Cys-His), which provides a link between the heme and the protein surface, where the redox partners of Cyt c bind. To elucidate the vibrational properties of heme c, nuclear resonance vibrational spectroscopy (NRVS) measurements were performed on (57)Fe-labeled ferric Hydrogenobacter t...
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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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Cytochromes c (Cyt c) are ubiquitous heme-containing proteins, mainly involved in electron transfer processes, whose structure and functions have been and still are intensely studied. Surprisingly, our understanding of the molecular mechanism whereby the heme group is covalently attached to the apoprotein (apoCyt) in the cell is still largely unknown. This posttranslational process, known as Cy...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2001
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.41.299