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T Mogi

Showing results (41-50 of 108) with videos related to

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FEBS Letters|September 3, 1999
Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygenT Mogi, M Sato-Watanabe, H Miyoshi, et al.
The Journal of Biological Chemistry|January 25, 1992
Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coliJ Minagawa, T Mogi, R B Gennis, et al.
Industrial Health|January 1, 1996
An endemic condition of biochemical hypoglycemia among male volunteersM Sasaki, T Mogi, Y Wada, et al.
The Journal of Biological Chemistry|April 22, 1994
Resonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centersT Uno, T Mogi, M Tsubaki, et al.
The Annals of Thoracic Surgery|May 1, 1976
Total rupture of the left main bronchus successfully repaired nine years after injuryA Nonoyama, A Masuda, K Kasahara, et al.
The Journal of Biological Chemistry|June 6, 1997
Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysisK Saiki, T Mogi, M Tsubaki, et al.
The Journal of Biological Chemistry|July 5, 1990
Transcriptional regulation of the cytochrome b562-o complex in Escherichia coli. Gene expression and molecular characterization of the promoterJ Minagawa, H Nakamura, I Yamato, et al.
Biochemical and Biophysical Research Communications|December 14, 1995
Characterization of chimeric heme-copper respiratory oxidases using subunits I of Escherichia coli cytochrome b o and Halobacterium salinarium cytochrome aa3K Denda, T Mogi, Y Anraku, et al.
Journal of Biochemistry|January 9, 1999
Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C analoguesH Miyoshi, K Takegami, K Sakamoto, et al.
FEBS Letters|August 21, 1995
CuB promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidaseT Mogi, T Hirano, H Nakamura, et al.
Pageof 11

Showing results (41-50 of 108) with videos related to

Sort By:
Pageof 11
FEBS Letters|September 3, 1999
Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygenT Mogi, M Sato-Watanabe, H Miyoshi, et al.
The Journal of Biological Chemistry|January 25, 1992
Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coliJ Minagawa, T Mogi, R B Gennis, et al.
Industrial Health|January 1, 1996
An endemic condition of biochemical hypoglycemia among male volunteersM Sasaki, T Mogi, Y Wada, et al.
The Journal of Biological Chemistry|April 22, 1994
Resonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centersT Uno, T Mogi, M Tsubaki, et al.
The Annals of Thoracic Surgery|May 1, 1976
Total rupture of the left main bronchus successfully repaired nine years after injuryA Nonoyama, A Masuda, K Kasahara, et al.
The Journal of Biological Chemistry|June 6, 1997
Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysisK Saiki, T Mogi, M Tsubaki, et al.
The Journal of Biological Chemistry|July 5, 1990
Transcriptional regulation of the cytochrome b562-o complex in Escherichia coli. Gene expression and molecular characterization of the promoterJ Minagawa, H Nakamura, I Yamato, et al.
Biochemical and Biophysical Research Communications|December 14, 1995
Characterization of chimeric heme-copper respiratory oxidases using subunits I of Escherichia coli cytochrome b o and Halobacterium salinarium cytochrome aa3K Denda, T Mogi, Y Anraku, et al.
Journal of Biochemistry|January 9, 1999
Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C analoguesH Miyoshi, K Takegami, K Sakamoto, et al.
FEBS Letters|August 21, 1995
CuB promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidaseT Mogi, T Hirano, H Nakamura, et al.
Pageof 11