@article {2438,
	title = {A DNAzyme with Three Protein-Like Functional Groups: Enhancing Catalytic Efficiency of M2+-Independent RNA Cleavage},
	journal = {Chembiochem},
	volume = {10},
	number = {12},
	year = {2009},
	note = {ISI Document Delivery No.: 487MWTimes Cited: 5Cited Reference Count: 76Hollenstein, Marcel Hipolito, Christopher J. Lam, Curtis H. Perrin, David M.},
	month = {Aug},
	pages = {1988-1992},
	type = {Article},
	keywords = {BEACON SENSOR, biology, CLEAVING DNA ENZYME, CYTOSOLIC FREE MAGNESIUM, DEOXYRIBOZYMES, DNAzymes, enzyme catalysis, EVOLUTION, HAIRPIN RIBOZYME, HIGH-DENSITY, IN-VITRO SELECTION, ION, nucleic acids, NUCLEIC-ACIDS, RNAse A mimics, synthetic},
	isbn = {1439-4227},
	url = {<Go to ISI>://000269279700012},
	author = {Hollenstein, M. and Hipolito, C. J. and Lam, C. H. and Perrin,David M.}
}
@article {2285,
	title = {Probing General Base Catalysis in the Hammerhead Ribozyme},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {46},
	year = {2008},
	note = {ISI Document Delivery No.: 406QZTimes Cited: 8Cited Reference Count: 53Thomas, Jason M. Perrin, David M.},
	month = {Nov},
	pages = {15467-15475},
	type = {Article},
	abstract = {Recent structural and computational studies have shed new light on the catalytic mechanism and active site structure of the RNA cleaving hammerhead ribozyme. Consequently, specific ribozyme functional groups have been hypothesized to be directly involved in general/acid base catalysis. In order to test this hypothesis, we have developed an affinity label to identify the functional general base in the S. mansoni hammerhead ribozyme. The ribozyme was reacted with a substrate analogue bearing a 2{\textquoteright}-bromoacetamide group in place of the nucleophilic 2{\textquoteright}-hydroxyl group which would normally be deprotonated by a general base. The electrophilic 2{\textquoteright}-bromoacetamide group is poised to alkylate the general base, which is subsequently identified by footprinting analysis. Herein, we demonstrate alkylation of N1 of G12 in the hammerhead ribozyme in a pH and [Mg2+] dependent manner that is consistent with the native cleavage reaction. These results provide substantial evidence that deprotonated N1 of G12 functions directly as a general base in the hammerhead ribozyme; moreover, our experiments provide evidence that the pK(a) of G12 is perturbed downward in the context of the active site structure. We also observed other pH-independent alkylations, which do not appear to reflect the catalytic mechanism, but offer further insight into ribozyme conformation and structure.},
	keywords = {ACTIVE-SITE, CLEAVAGE, CRYSTAL-STRUCTURE, DELTA VIRUS RIBOZYME, HAIRPIN RIBOZYME, MECHANISM, METAL-ION, MONOVALENT CATIONS, NUCLEOBASE CATALYSIS, RNA},
	isbn = {0002-7863},
	url = {<Go to ISI>://000263311300051},
	author = {Thomas, J. M. and Perrin,David M.}
}
