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oai:www.ideals.illinois.edu:2142/84824 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gennis, Robert B. Han, Dan 2015-09-25T22:28:05Z 2015-09-25T22:28:05Z 10000-01-01 2006 2006 The monomeric form of bovine heart mitochondrial cytochrome c oxidase was used to detect directly the proton uptake and release events during the F-to-O transition. Absorption change of the pH sensitive dye was monitored spectroscopically. Rapid proton release followed by slow proton uptake was observed. This result indicates that both the pumped protons and the protons required for chemistry at the active site might come from an internal proton pool containing at least two protons. Made available in DSpace on 2015-09-25T22:28:05Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3223606.pdf: 3773004 bytes, checksum: 58abdb06f7233cde016072639cbe5942 (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 86105 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 192 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/84824 (MiAaPQ)AAI3223606 eng Chemistry, Biochemistry Studies on the Proton Pumping Mechanism of Aa(3)-Type Cytochrome C Oxidase text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.