T Mogi
Overview
Explore the profile of T Mogi including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
108
Citations
1274
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Ozawa K, Mogi T, Suzuki M, Kitamura M, Nakaya T, Anraku Y, et al.
Anaerobe
. 2006 Aug;
3(5):339-46.
PMID: 16887609
Cytoplasmic membranes were isolated from the cells of a sulfate-reducing strict anaerobe Desulfovibrio vulgaris Miyazaki F and membrane-bound cytochromes were characterized. Redox difference spectra at 77 K revealed the presence...
2.
Grimaldi S, Ostermann T, Weiden N, Mogi T, Miyoshi H, Ludwig B, et al.
Biochemistry
. 2003 May;
42(19):5632-9.
PMID: 12741819
Ubiquinone-2 (UQ-2) selectively labeled with (13)C (I =(1)/(2)) at either the position 1- or the 4-carbonyl carbon is incorporated into the ubiquinol oxidase bo(3) from Escherichia coli in which the...
3.
Fujimori F, Gunji W, Kikuchi J, Mogi T, Ohashi Y, Makino T, et al.
Biochem Biophys Res Commun
. 2001 Nov;
289(1):181-90.
PMID: 11708797
Previous studies have indicated that Ess1/Pin1, a gene in the parvulin family of peptidyl-prolyl isomerases (PPIases), plays an important role in regulating the G(2)/M transition of the cell cycle by...
4.
Tsubaki M, Hori H, Mogi T
J Inorg Biochem
. 2001 Jan;
82(1-4):19-25.
PMID: 11132627
Cytochromes bo and bd are structurally unrelated terminal ubiquinol oxidases in the aerobic respiratory chain of Escherichia coli. The high-spin heme o-CuB binuclear center serves as the dioxygen reduction site...
5.
Kobayashi K, Tagawa S, Mogi T
Biochemistry
. 2000 Dec;
39(50):15620-5.
PMID: 11112550
To elucidate a unique mechanism for the quinol oxidation in the Escherichia coli cytochrome bo, we applied pulse radiolysis technique to the wild-type enzyme with or without a single bound...
6.
Uchida T, Mogi T, Kitagawa T
Biochemistry
. 2000 Jun;
39(22):6669-78.
PMID: 10828985
Cytochrome bo from Escherichia coli, a member of the heme-copper terminal oxidase superfamily, physiologically catalyzes reduction of O(2) by quinols and simultaneously translocates protons across the cytoplasmic membrane. The reaction...
7.
Hellwig P, Mogi T, Tomson F, Gennis R, Iwata J, Miyoshi H, et al.
Biochemistry
. 1999 Nov;
38(44):14683-9.
PMID: 10545194
In this study we present the infrared spectroscopic characterization of the bound ubiquinone in cytochrome bo(3) from Escherichia coli. Electrochemically induced Fourier transform infrared (FTIR) difference spectra of DeltaUbiA (an...
8.
Sakamoto K, Mogi T, Noguchi S, Sone N
J Biochem
. 1999 Nov;
126(5):934-9.
PMID: 10544288
To probe the location of the quinol oxidation site and physical interactions for inter-subunit electron transfer, we constructed and characterized two chimeric oxidases in which subunit II (CyoA) of cytochrome...
9.
Mogi T, Miyoshi H, Orii Y
FEBS Lett
. 1999 Sep;
457(1):61-4.
PMID: 10486564
To probe the functional role of a bound ubiquinone-8 in cytochrome bo-type ubiquinol oxidase from Escherichia coli, we examined reactions with ubiquinol-1 and dioxygen. Stopped-flow studies showed that anaerobic reduction...
10.
Mogi T, Miyoshi H, Orii Y
FEBS Lett
. 1999 Sep;
457(2):223-6.
PMID: 10471783
To probe the functional role of a bound ubiquinone-8 in cytochrome bo-type ubiquinol oxidase from Escherichia coli, we examined reactions with ubiquinol-1 and dioxygen. Stopped-flow studies showed that anaerobic reduction...