Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Futoshi Masuya"'
Autor:
Futoshi Masuya, Yoko Ariga, Masashi Unno, Tsuyoshi Egawa, Hiroshi Hori, Yuzuru Ishimura, Hideo Shimada, Shingo Nagano, Takashi Obata, Takako Hishiki
Publikováno v:
Journal of Biological Chemistry. 274:9363-9369
During the monooxygenase reaction catalyzed by cytochrome P450cam (P450cam), a ternary complex of P450cam, reduced putidaredoxin, andd-camphor is formed as an obligatory reaction intermediate. When ligands such as CO, NO, and O2 bind to the heme iron
Autor:
Shigetoshi Miura, Hiroshi Hori, Kohji Morimoto, Motonari Tsubaki, Futoshi Masuya, Akira Miyatake, Shuhei Tomita, Yoshiyuki Ichikawa
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1259:89-98
Cytochrome P-450c21 (CYP21A1) purified from bovine adrenocortical microsomes was investigated by electron paramagnetic resonance (EPR) spectroscopy to clarify the interactions among heme active center, protein surroundings, water molecules and bound
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
Publikováno v:
Journal of Biological Chemistry. 267:18377-18381
Low temperature photolysis of nitric oxide from the nitrosyl complexes of ferric cytochrome P450scc was examined by EPR spectroscopy to elucidate the stereochemical interaction between heme-bound ligand and side-chain of cholesterol or its hydroxylat
Publikováno v:
Journal of biochemistry. 130(6)
The cholesterol side-chain cleavage reaction catalyzed by cytochrome P450scc comprises three consecutive monooxygenase reactions (22R-hydroxylation, 20S-hydroxylation, and C 2 0 -C 2 2 bond scission) that produces pregnenolone. The electron equivalen
Publikováno v:
Journal of inorganic biochemistry. 82(1-4)
The nitrosyl complex of ferric myoglobin is EPR-silent. Upon photolysis at low temperatures, the photoinduced intermediates trapped in the distal heme cavity exhibit new EPR spectra due to the interaction between the photodissociated NO (S=1/2) and t
Autor:
Hiroshi Hori, Yuzuru Ishimura, Yoko Kimata, R Makino, Masashi Unno, Hideo Shimada, Takashi Obata, Futoshi Masuya
Publikováno v:
Oxygen Homeostasis and Its Dynamics ISBN: 9784431684787
P-450cam catalyzes the conversion of d-camphor to 5-exo-hydroxycamphor at the expense of 1 mole each of NADH and oxygen. Two reducing equivalents from NADH are transferred to P-450cam via two redox-linked proteins, putidaredoxin reductase (PdR) and p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::706284ebce3a958f8b3819389dfcdc75
https://doi.org/10.1007/978-4-431-68476-3_16
https://doi.org/10.1007/978-4-431-68476-3_16
Autor:
Hiroshi Hori, Futoshi Masuya
Publikováno v:
Biochimica et biophysica acta. 1203(1)
Manganese(II) protoporphyrin-IX substituted myoglobin with site-specifically cyanated or N-tetrazolated distal histidine (His) was prepared and low-temperature photolysis of nitric oxide (NO) from their nitrosyl complexes was examined by electron par