منابع مشابه
A functioning complex between tryptic fragments of cytochrome c. A route to the production of semisynthetic analogues.
We report the discovery of a functioning non-covalent complex between two peptides obtained from a limited tryptic digest of horse heart cytochrome c. We have used the phenomenon to produce three modified versions of the complex. We have replaced lysine-39 semisynthetically with ornithine in the first analogue, with p-fluorophenyl-alanine in the second, and removed it entirely in the third.
متن کاملCytochrome c
How is it made? Cytochrome c is synthesized from two inactive precursor molecules: apocytochrome c (a protein that is encoded by a nuclear gene and imported into mitochondria) and heme (which is synthesized in mitochondria). The covalent attachment of apocytochrome c to heme is catalyzed by heme lyase and creates cytochrome c, a 14.5 kDa protein that is normally confined to the intermembrane sp...
متن کاملThe cytochrome c binding site on cytochrome c oxidase.
Cytochrome c oxidase (EC 1.9.3.1) is the terminal enzyme of the mitochondria respiratory chain catalysing electron transfer from cytochrome c to molecular oxygen [ 1,2]. The molecular mechanism of this process is still not understood. At present, little is known about such important structural features as the position of the prosthetic groups or the location and characteristics of the cytochrom...
متن کاملModified Deacetylcephalosporin C Synthase for the Biotransformation of Semisynthetic Cephalosporins.
UNLABELLED Deacetylcephalosporin C synthase (DACS), a 2-oxoglutarate-dependent oxygenase synthesized by Streptomyces clavuligerus, transforms an inert methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) during the biosynthesis of cephalosporin. It is a step which is chemically difficult to accomplish, but its development by use of an en...
متن کاملThe Cytochrome C-cytochrome Oxidase Complex
In the preceding paper the oxidation of substrates by “indophenol oxidase” was demonstrated to be a joint action of cytochrome and cytochrome oxidase. It was further shown that with a given amount of oxidase the velocity of hydroquinone oxidation reached a maximum as the amount of added cytochrome was increased. The latter fact immediately suggested the probability that the rapid aerobic oxidat...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1977
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.74.10.4248