Mechanistic studies of the class I ribonucleotide reductases from S. cerevisiae and E. coli.

(cont.) The results of initial studies on the energetics of heterodimer formation using calorimetric techniques and site-directed mutagenesis are discussed in the context of the structures of Y2Y2, Y2Y4, and Y4Y4. As the discovery of a second R2 subunit is not unique to S. cerevisiae, the potential implication of the heterodimer in the regulation of deoxyribonucleotide synthesis is also considered. In the second part of this thesis, pre-steady state kinetics of the class I E. coli RNR is investigated using stopped-flow UV-visible spectroscopy and rapid chemical quench methods. These studies have led to a model in which the rate determining step in catalysis is a physical step prior to proton-coupled electron transfer (PCET), nucleotide reduction, and reverse PCET. These results provide a crucial first step in understanding radical initiation over 35 [angstroms].

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Chemistry.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2003

Author dc:creator

• Ge, Jie, 1976-

Advisor dc:contributor.advisor

• JoAnne Stubbe.

• Chemistry.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

en_US

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/27372

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/27372