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oai:www.ideals.illinois.edu:2142/84783 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gennis, Robert B. Zhou, Weidong 2015-09-25T22:27:52Z 2015-09-25T22:27:52Z 10000-01-01 2002 2002 In the NqrF subunit, four conserved cysteines (C70, C76, C79 and C111) are predicted to ligate the 2Fe-2S center, and three conserved residues (R210, Y212, S245) are predicted to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center. Made available in DSpace on 2015-09-25T22:27:52Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3044275.pdf: 7580857 bytes, checksum: 5e74ad061a37bbcd9e69be29d58e9203 (MD5) Previous issue date: 2002 Embargo set by: Seth Robbins for item 86064 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 187 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2002. http://hdl.handle.net/2142/84783 (MiAaPQ)AAI3044275 eng Biophysics, General Biochemical Studies of the Sodium -Translocating NADH:ubiquinone Oxidoreductase text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.