47310-09-8

Upstream product

• 501-53-1 benzyl chloroformate 
• 99-31-0 5-aminoisophthalic acid 
• 153233-30-8 5-(benzyloxycarbonylamino)isophthalic acid 

Downstream Products

• 208251-78-9 {[3-Benzyloxycarbonylamino-5-(bis-ethoxycarbonylmethyl-carbamoyl)-benzoyl]-ethoxycarbonylmethyl-amino}-acetic acid ethyl ester 
• 1330777-01-9 BrH*C₅₆H₆₉N₇O₂₂ 
• 1330777-00-8 C₆₄H₇₅N₇O₂₄ 

Relevant academic research and scientific papers

Precise design of artificial cofactors for enhancing peroxidase activity of myoglobin: Myoglobin mutant H64D reconstituted with a "single-winged cofactor" Is equivalent to native horseradish peroxidase in oxidation activity

H64D myoglobin mutant was reconstituted with two different types of synthetic hemes that have aromatic rings and a carboxylate-based cluster attached to the terminus of one or both of the heme-propionate moieties, thereby forming a "single-winged cofactor" and "double-winged cofactor," respectively. The reconstituted mutant myoglobins have smaller Km values with respect to 2-methoxyphenol oxidation activity relative to the parent mutant with native heme. This suggests that the attached moiety functions as a substrate-binding domain. However, the kcat value of the mutant myoglobin with the double-winged cofactor is much lower than that of the mutant with the native heme. In contrast, the mutant reconstituted with the single-winged cofactor has a larger kcat value, thereby resulting in overall catalytic activity that is essentially equivalent to that of the native horseradish peroxidase. Enhanced peroxygenase activity was also observed for the mutant myoglobin with the single-winged cofactor, thus indicating that introduction of an artificial substrate-binding domain at only one of the heme propionates in the H64D mutant is the optimal engineering strategy for improving the peroxidase activity of myoglobin. Copyright

Artificial protein-protein complexation between a reconstituted myoglobulin and cytochrome c

Artificial prosthetic porphyrins, 1·Fe and 1·Zn, in which two isophthalamide units having four carboxylates were bound to the terminal of each pripheral propionate side chain in protoporhyrin IX, were inserted into horse heart apomyoglobin to give novel mylglobins rMb(1·Fe) and rMb(1·Zn), respectively. The resultant reconstituted myoglobins were designed to bind cationic cytochrome c on the protein surface via elecrostatic interaction. The isoelectric point for rMB(1·Fe) was determined to be 5.5, which is about 2 pH units lower than that of native myoglobin. The pI value suggests that eight carboxylates of prosthetic group are located on the surface of the myoglobin. A construction of a myoglobin-cytochrome c complex was probed by paramagnetic 1H NMR and flash photolysis studies. The behavior of 1H NMR paramagnetic shifts in the rMb(1·FeCN) cytochrome c complex is comparable with that in the native pairing of cytochrome c-cytochrome c peroxidase. Laser flash photolysis shows that a long-range ET from photoexcited rMb- (1·Zn) to cytochrome coccurs within the protein-protein complex. The time- dependence of the transient spectra at 460 nm identified as the triplet excited state of rMb(1·Zn) leads to rate constant of forward ET and affinity of the protein-protein complex; k(intra) = (2.2 ± 0.1) x 103 s-1 and K(a) = (6.5 ± 3.0) x 104 M-1 at 10 mM ionic strength and k(intra) = (2.3 ± 0.2) x 103 s-1 and K(a) = (1.5 + 0.6) x 104 M-1 at 20 Mm ionic strength and pH 7.0. The binding affinity for cytochrome c decreases with increasing te ionic strength, indicating that the protein-protein complex is formed by elecrostatic interaction. This work demonstrates that the artificial functional groups bound to the terminal of porphyrin in the reconstituted myoglobin can act as an effective recognition domain for a protein at the surface of the myoglobin.