Kodadek

Other clues to the self-association of recombinant resilin in solution, and thus a degree of defined stmcture, include the propensity of the monomer proteins to covalently cross-link very rapidly through dityrosine side chains using a mthenium-based photochemical method [29]. Proteins which do not naturally self-associate do not form biomaterials when exposed to the Ru(ll)-based photochemical procedure (Elvin, C.E. and Brownlee, A.G., personal communication). Furthermore, Kodadek and colleagues showed that only intimately associated proteins are cross-linked via this zero-A photochemistry procedure [45]. 

Fancy, D.A. and Kodadek, T., Chemistry for the analysis of protein-protein interactions Rapid and efficient cross-linking triggered by long wavelength light, Proc. Natl. Acad. Sci. USA, 96, 6020-6024, 1999. 

Amini, F., Denison, C., Lin, H.J., Kuo, L., and Kodadek, T., Using oxidative crosslinking and proximity labelling to quantitatively characterize protein-protein and protein-peptide complexes, Chem. Biol., 10(11), 1115-1127, 2003. 

In 1980 and 1982, Callot and co-workers reported that Rh(Por)l catalyzed the reaction between alkenes and ethyl diazoacetate to give syn cyclopropoanes as the major products (Eq. 25). " This was unusual as most transition metal catalysts for this reaction give the anti isomers as the predominant products. Kodadek and co-workers followed up this early report and put considerable effort into trying to improve the syn/anti ratios and enantioselectivity using porphyrins with chiral substituents. 

To simplify the catalytic system further, Kodadek and Woo investigated the activity of [Fe(F2o-TPP)Cl] for alkene cyclopropanation with EDA in the absence of cobaltocene. These workers proposed that electron-deficient porphyrin would render the Fe(III) porphyrin more easily reduced by EDA. Indeed, [Fe(F2o-TPP)Cl] efficiently catalyzes alkene cyclopropanation with EDA with high catalyst turnover... 

Kodadek, T. (2001), Protein microarrays prospects and problems , Chem. Biol., 8, 105 -115. 

Dordick, 1991). In addition, Fancy et al. (1996) as well as Fancy and Kodadek (1997, 1998) have applied the oxidation of tyrosine to form dityrosine to the study of protein-protein interactions using nickel-chelated 6 X His tagged fusion proteins in oxidative environments. 

Fancy, D.A., and Kodadek, T. (1998) A critical role for tyrosine residues in His6Ni-mediated protein crosslinking. Biochem. Biophys. Res. Comm. 247, 420-426. 

Kodadek, T. Physical association of the APIS complex and general transcription factors. Biochem. Biophys. Res. Commun. 2002, 296, 991-999. 

---