Zobrazeno 1 - 10
of 195
pro vyhledávání: '"Yuzuru, Ishimura"'
Autor:
Tetsutaro Iizuka, Keisuke Mashima, Yuzuru Ishimura, R Makino, Hiroshi Hori, Eiji Obayashi, Yoshitsugu Shiro
Publikováno v:
Biochemistry. 54:3604-3616
L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O₂ into the pyrrole ring of L-tryptophan. Although a ferrous-oxy form (Fe²⁺-O₂) has been established to be an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e1477e17a65a20130019819a0387907
https://doi.org/10.1021/acs.biochem.5b00048
https://doi.org/10.1021/acs.biochem.5b00048
Autor:
P.D. BRAGG, J.J. BULLEN, R.H. BURRIS, B.R. BYERS, Jiann-Shin CHEN, ROGER A. CLEGG, CHARLES N. DAVID, THOMAS EMERY, E. GRIFFITHS, YUZURU ISHIMURA, WARREN P. IVERSON, NICHOLAS J. JACOBS, P. ANN LIGHT, WALTER LOVENBERG, D.G. LUNDGREN, RICHARD E. MILLER, LEONARD E. MORTENSON, J.B. NEILANDS, MITSUHIRO NOZAKI, K. OKUNIKI, W.H. ORME-JOHNSON, HENRY J. ROGERS, H. ROSENBERG, RICHARD D. SAGERS, STANLEY L. STREICHER, F.R. TABITA, RAYMOND C. VALENTINE, J.R. VESTAL, T. YAMANAKA, TAKASHI YONETANI, I.G. YOUNG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c4bf692911bc6ede9dc8a18610c7f3
https://doi.org/10.1016/b978-0-08-100449-4.09990-5
https://doi.org/10.1016/b978-0-08-100449-4.09990-5
Autor:
Ying Tong Gao, Pavel Martásek, Bettie Sue Siler Masters, Yuzuru Ishimura, Satya Prakash Panda, Linda J. Roman
Publikováno v:
Journal of Biological Chemistry. 282:28557-28565
Nitric-oxide synthase (NOS) catalyzes both coupled and uncoupled reactions that generate nitric oxide and reactive oxygen species. Oxygen is often the overlooked substrate, and the oxygen metabolism catalyzed by NOS has been poorly defined. In this p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2ddd876d720571ed54a939c2dd8aea1
https://doi.org/10.1074/jbc.m704890200
https://doi.org/10.1074/jbc.m704890200
Autor:
Ryu, Makino, Eiji, Obayashi, Hiroshi, Hori, Tetsutaro, Iizuka, Keisuke, Mashima, Yoshitsugu, Shiro, Yuzuru, Ishimura
Publikováno v:
Biochemistry. 54(23)
L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O₂ into the pyrrole ring of L-tryptophan. Although a ferrous-oxy form (Fe²⁺-O₂) has been established to be an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e048e0da252811ce3b04376824d2d2ee
https://pubmed.ncbi.nlm.nih.gov/25996254
https://pubmed.ncbi.nlm.nih.gov/25996254
Autor:
Ying Tong Gao, Satya Prakash Panda, Bettie Sue Siler Masters, Yuzuru Ishimura, Linda J. Roman, Susan T. Weintraub
Publikováno v:
Biochemical and Biophysical Research Communications. 338:543-549
Using headspace gas chromatography–mass spectrometry, we detected significant amounts of nitrous oxide in the reaction products of the monooxygenase reaction catalyzed by neuronal nitric oxide synthase. Nitrous oxide is a dimerization product of ni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a348d6b8bdb693e6bbce25cef2f56e
https://doi.org/10.1016/j.bbrc.2005.07.202
https://doi.org/10.1016/j.bbrc.2005.07.202
Autor:
Satya Prakash Panda, Yuzuru Ishimura, Bettie Sue Siler Masters, Markandeswar Panda, Jung-Ja P. Kim, M. Jáchymová, Linda J. Roman, Thomas M. Shea, Pavel Martásek
Publikováno v:
Proceedings of the National Academy of Sciences. 102:15833-15838
At least three building blocks are responsible for the molecular basis of the modulation of electron transfer in nitric oxide synthase (NOS) isoforms: the calmodulin-binding sequence, the C-terminal extension, and the autoregulatory loop in the reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8209822c2274e0cf8197227def5de0ca
https://doi.org/10.1073/pnas.0506522102
https://doi.org/10.1073/pnas.0506522102
Autor:
Tsuyoshi Egawa, Hideo Shimada, Satoshi Takahashi, Takako Hishiki, Yusuke Ichikawa, Teizo Kitagawa, Yasukazu Kanamori, Yuzuru Ishimura
Publikováno v:
Journal of Biological Chemistry. 279:32008-32017
Changes in heme coordination state and protein conformation of cytochrome P450cam (P450cam), a b-type heme protein, were investigated by employing pH jump experiments coupled with time-resolved optical absorption, fluorescence, circular dichroism, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c81b04696910b229a92cf289154e9e0
https://doi.org/10.1074/jbc.m310810200
https://doi.org/10.1074/jbc.m310810200
This first volume in a projected series contains the proceedings of the first of the Keio University International Symposia for Life Sciences and Medicine under the sponsorship of the Keio University Medical Science Fund. As stated in the address by
Autor:
Tsunehiko Higuchi, Teizo Kitagawa, Hideo Shimada, Tsuyoshi Egawa, Noriyuki Suzuki, Takashi Dokoh, Yuzuru Ishimura
Publikováno v:
The Journal of Physical Chemistry A. 108:568-577
Resonance Raman spectra were observed for heme proteins and iron(II) porphyrins including ferrous-CO and ferrous-isocyanide derivatives of cytochrome P450cam, a synthetic iron(II) porphyrin complex having a thiolate axial ligand, ferrous-isocyanide d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9859bd061e315f0a8a30d88d9837d25b
https://doi.org/10.1021/jp0355612
https://doi.org/10.1021/jp0355612
Autor:
Yoshitsugu Shiro, Yoko Kimata-Ariga, Tsuyoshi Egawa, Sam-Yong Park, Yuzuru Ishimura, Takako Hishiki, Shin-ichi Adachi, Akiko Tarumi, Hideo Shimada, Makoto Suematsu, Shingo Nagano
Publikováno v:
Biochemistry. 42:14507-14514
Ferrous-carbon monoxide bound form of cytochrome P450cam (CO-P450cam) has two infrared (IR) CO stretching bands at 1940 and 1932 cm - 1 . The former band is dominant (>95% in area) for CO-P450cam free of putidaredoxin (Pdx), while the latter band is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2100eb9e300e7c4f26f7414ddb6c9868
https://doi.org/10.1021/bi035410p
https://doi.org/10.1021/bi035410p