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T Mogi

Showing results (81-90 of 108) with videos related to

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The Journal of Biological Chemistry|November 18, 1994
Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenolsM Sato-Watanabe, T Mogi, H Miyoshi, et al.
The Journal of Biological Chemistry|November 18, 1994
Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coliM Sato-Watanabe, T Mogi, T Ogura, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1990
Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsinD J Jang, M A el-Sayed, L J Stern, et al.
The Journal of Biological Chemistry|April 15, 1991
Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocationT Marti, H Otto, T Mogi, et al.
Biophysical Journal|May 1, 1992
Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsinS Wu, Y Chang, M A el-Sayed, et al.
Biochemistry|November 15, 1988
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212M S Braiman, T Mogi, T Marti, et al.
Biochemistry|October 28, 1998
Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidaseK Sakamoto, H Miyoshi, M Ohshima, et al.
The Journal of Biological Chemistry|September 25, 1988
Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopyP L Ahl, L J Stern, D Düring, et al.
Biochemistry|November 5, 1999
Vibrational modes of ubiquinone in cytochrome bo(3) from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific (13)C labelingP Hellwig, T Mogi, F L Tomson, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsinH Otto, T Marti, M Holz, et al.
Pageof 11

Showing results (81-90 of 108) with videos related to

Sort By:
Pageof 11
The Journal of Biological Chemistry|November 18, 1994
Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenolsM Sato-Watanabe, T Mogi, H Miyoshi, et al.
The Journal of Biological Chemistry|November 18, 1994
Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coliM Sato-Watanabe, T Mogi, T Ogura, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1990
Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsinD J Jang, M A el-Sayed, L J Stern, et al.
The Journal of Biological Chemistry|April 15, 1991
Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocationT Marti, H Otto, T Mogi, et al.
Biophysical Journal|May 1, 1992
Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsinS Wu, Y Chang, M A el-Sayed, et al.
Biochemistry|November 15, 1988
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212M S Braiman, T Mogi, T Marti, et al.
Biochemistry|October 28, 1998
Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidaseK Sakamoto, H Miyoshi, M Ohshima, et al.
The Journal of Biological Chemistry|September 25, 1988
Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopyP L Ahl, L J Stern, D Düring, et al.
Biochemistry|November 5, 1999
Vibrational modes of ubiquinone in cytochrome bo(3) from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific (13)C labelingP Hellwig, T Mogi, F L Tomson, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsinH Otto, T Marti, M Holz, et al.
Pageof 11