Incorporation into acid clusters

These mechanisms ascribe in jortance to the Lewis acid-Lewis base interaction between the allyl halide and the organolithium reagent. When substitution is complete, the halide ion is incorporated into the lifliium cluster in place of one of the carbon ligands. 

The Rieske protein in mitochondrial bci complexes is assembled when the protein is incorporated into the complex. The Rieske protein is encoded in the nucleus and synthesized in the cytosol with a mitochondrial targeting presequence, which is required to direct the apoprotein to the mitochondrial matrix. The C-terminus is then targeted back to the outside of the inner mitochondrial membrane where the Rieske cluster is assembled. In addition, the presequence is removed and the protein is processed to its mature size after the protein is inserted into the bci complex. In mammals, the presequence is cleaved in a single step by the core proteins 1 and 2, which are related to the general mitochondrial matrix processing protease (MPP) a and (3 subunits the bovine heart presequence is retained as a 8.0 kDa subunit of the complex (42, 107). In Saccharomyces cerevis-iae, processing occurs in two steps Initially, the yeast MPP removes 22 amino acid residues to convert the precursor to the intermediate form, and then the mitochondrial intermediate protease (MIP) removes 8 residues after the intermediate form is in the bci complex (47). Cleavage by MIP is independent of the assembly of the Rieske cluster Conversion of the intermediate to the mature form was observed in a yeast mutant that did not assemble any Rieske cluster (35). However, in most mutants where the assembly of the Rieske cluster is prevented, the amount of Rieske protein is drastically reduced, most likely because of instability (35, 44). 

Figure 11.5 Amino acid building blocks are incorporated into daptomycin backbone successively by NRPS subunits DptA, DptBC and DptD (a). Structural diversity of daptomycin peptide core can be obtained by genetic modifications of dpt gene cluster (b). C, condensation domain A, adenylation domain PCP, peptidyl carrier protein E, epimerase TE, thioesterase domain... 

The bifunctional zeolite catalysts are composed of both acid sites and metal clusters. The preparation methods of these catalysts encompasses three steps ion exchange, calcination, and reduction. The ion-exchange process is carried out with aqueous solutions of salts or, more commonly, of complexes of the metals that will be incorporated into the zeolite cavities and channels. 

These procedures have been used to create a number of peptide clusters with over 65 amino acid residues. A common motif for forming these clusters is the ferredoxin consensus sequence (6) (Figure 7) incorporated into a longer chain or even peptide sequences with additional secondary structure. 

PQQ is derived from a peptide precursor that contains conserved glutamate (13) and tyrosine (76) residues. All carbon and nitrogen atoms of the precursor amino acids are incorporated into the product (44). Gene clusters involved in this pathway have been studied in considerable detail. The X-ray structure of the enzyme that catalyzes the final reaction step has been determined, and reaction mechanisms have been proposed on that basis (45). However, details of the biosynthetic pathway are still incompletely understood. 

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