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Initial O₂ Insertion Step of the Tryptophan Dioxygenase Reaction Proposed by a Heme-Modification Study

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

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X-Ray Crystal Structure and Catalytic Properties of Thr252Ile Mutant of Cytochrome P450cam: Roles of Thr252 and Water in the Active Center

Autor: Shingo Nagano, Sam-Yong Park, Yasukazu Kanamori, Yoshitsugu Shiro, Takako Hishiki, Shin-ichi Adachi, Hideo Shimada, Yuzuru Ishimura, Tsuyoshi Egawa, Ryu Makino

Publikováno v: Journal of Biochemistry. 128:965-974

The structure-function relationship in cytochrome P450cam monooxygenase was studied by employing its active site mutant Thr252Ile. X-ray crystallographic analyses of the ferric d-camphor-bound form of the mutant revealed that the mutation caused a st

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::488ff932d5c6ddf1d0f20d5683485893
https://doi.org/10.1093/oxfordjournals.jbchem.a022848

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Role of Arg112 of Cytochrome P450cam in the Electron Transfer from Reduced Putidaredoxin

Autor: Yuzuru Ishimura, Hideo Shimada, Yoko Toba, Ryu Makino, Masashi Unno

Publikováno v: Journal of Biological Chemistry. 271:17869-17874

The mechanism for the reduction of ferric cytochrome P450cam by reduced putidaredoxin, the physiological electron donor for the cytochrome, has been studied by using site-directed mutants of cytochrome P450cam, in which Arg112, an amino acid residue

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a21f4e992c769c9e533c028eadff4d06
https://doi.org/10.1074/jbc.271.30.17869

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The Structure−Function Relationship and Reduction Potentials of High Oxidation States of Myoglobin and Peroxidase

Autor: Bruce R. Copeland, Bing He, Linda S. Powers, R. Sinclair, Ryu Makino, I. Yamazaki

Publikováno v: Biochemistry. 35:2413-2420

In these studies, we substitute electron-withdrawing (diacetyl) or -donating (diethyl) groups at the 2- and 4-positions of the heme in sperm whale Mb and HRP, and examine the structural and biochemical consequences. X-ray absorption spectroscopy show

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93558c34ebbabe7ef764be423f690746
https://doi.org/10.1021/bi952365f

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Thermodynamic aspects of the CO-binding reaction to cytochrome P-450cam. Relevance with their biological significance and structure

Autor: Minoru Kato, Ryu Makino, Tetsutaro Iizuka

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1246:178-184

The CO-binding kinetics of cytochrome P-450cam(+) and P-450cam(−) have been measured in the millisecond time domain using a flash photolysis method. We have determined the reaction coordinates for free energy, enthalpy and entropy from the temperat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72855a80b8b8a39fc6f64b0f09315ac5
https://doi.org/10.1016/0167-4838(94)00197-o

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EPR Studies on the Photoproducts of Ferric Cytochrome P450cam (CYP101) Nitrosyl Complexes: Effects of Camphor and Its Analogues on Ligand-Bound Structures1

Autor: Ryu Makino, Motonari Tsubaki, Futoshi Masuya, Hiroshi Hori

Publikováno v: The Journal of Biochemistry. 116:1146-1152

Photolyzed products of the NO complexes of ferric cytochrome P450cam both in the substrate-free and several substrate-bound states were trapped and examined by EPR spectroscopy at 5 K. In the absence of substrate, the photoproduct exhibited ferric hi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ca415da0f46c9f07ebd2e077b076a09f
https://doi.org/10.1093/oxfordjournals.jbchem.a124641

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