Výsledky vyhledávání - "Nobuhito Sone"

Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3

Autor: Junshi Sakamoto, Nobuhito Sone, Yoshiki Kabashima, Tomoichirou Kusumoto

Publikováno v: Journal of Bioenergetics and Biomembranes. 45:131-136

Several bacteria possess membrane-bound dehydrogenases other than cytosolic dehydrogenases in their respiratory chains. In many cases, the membrane-bound malate:quinone oxidoreductases (MQOs) are essential for growth. However, these MQOs are absent i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce1ef577126c505cea5fe99ba4005ce1
https://doi.org/10.1007/s10863-012-9485-5

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Essential arginine residue of the Fo-a subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel

Autor: Sakurako Ono, Masasuke Yoshida, Nobuhito Sone, Noriyo Mitome, Hiroki Sato, Toshiharu Suzuki

Publikováno v: Biochemical Journal. 430:171-177

In F(o)F(1) (F(o)F(1)-ATP synthase), proton translocation through F(o) drives rotation of the oligomer ring of F(o)-c subunits (c-ring) relative to F(o)-a. Previous reports have indicated that a conserved arginine residue in F(o)-a plays a critical r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f773567f99605c08a5c1f7ddbcfcb10
https://doi.org/10.1042/bj20100621

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ATP Synthase that Lacks F0a-Subunit

Autor: Sakurako Ono, Nobuhito Sone, Toshiharu Suzuki, Masasuke Yoshida

Publikováno v: Journal of Biological Chemistry. 279:33409-33412

In a rotary motor F1F0-ATP synthase, F0 works as a proton motor; the oligomer ring of F0c-subunits (c-ring) rotates relative to the F0ab2 domain as protons pass through F0 down the gradient. F0ab2 must exert dual functions during rotation, that is, s

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https://doi.org/10.1074/jbc.m404993200

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Transient association of the sarcoplasmic reticulum Ca2+ATPase with the Na+/K+-ATPase and H+/K+-ATPase β-subunits during its biogenesis in Xenopus oocytes

Autor: Masaru Kawamura, Nobuhito Sone, Shunsuke Noguchi

Publikováno v: Journal of Cell Science. 116:1875-1880

We examined the effect of the β-subunits of the Na + /K + and H + /K + ATPases on the biogenesis of the sarcoplasmic reticulum (SR) Ca 2+ ATPase in Xenopus oocytes. Oocytes were simultaneously injected with cRNAs for both the SR Ca 2+ ATPase and the

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https://doi.org/10.1242/jcs.00392

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Improved H+/O Ratio and Cell Yield of Escherichia coli with Genetically Altered Terminal Quinol Oxidases

Autor: Shinji Minohara, Nobuhito Sone, Junshi Sakamoto

Publikováno v: Journal of Bioscience and Bioengineering. 93:464-469

Escherichia coli wild-type cells, containing both cytochrome bo- and bd-type terminal oxidases, pumped protons with a H+/O ratio of 4.5–4.9 upon an oxygen pulse, while mutant cells, deprived of either cytochrome bo (Δcyo) or bd (Δcyd), showed val

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https://doi.org/10.1263/jbb.93.464

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Cytochrome c oxidase contains an extra charged amino acid cluster in a new type of respiratory chain in the amino-acid-producing Gram-positive bacterium Corynebacterium glutamicum The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are AB052748 and AB052749

Autor: Ryoko Miyahara, Shunsuke Noguchi, Kazunobu Matsushita, Tomokimi Torigoe, Junshi Sakamoto, Takatsugu Shibata, Nobuhito Sone, Tadashi Mine

Publikováno v: Microbiology. 147:2865-2871

The membranes from Corynebacterium glutamicum cells contain a hydrophobic di-haem C protein as the cytochrome c subunit of the new type of cytochrome bc complex (complex III in the respiratory chain) encoded by the qcrCAB operon [Sone, N., Nagata, K.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::01bdc3fae47ad9e2e24556fcc978004e
https://doi.org/10.1099/00221287-147-10-2865

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Inhibitory Activities of Lansoprazole against Respiration in Helicobacter pylori

Autor: Kumiko Nagata, Toshihide Tamura, Nobuhito Sone

Publikováno v: Antimicrobial Agents and Chemotherapy. 45:1522-1527

Lansoprazole and its derivative AG-1789 dose-dependently inhibited cellular respiration by an endogenous substrate and decreased the ATP level in Helicobacter pylori cells. The inhibitory action of lansoprazole and AG-1789 against respiration was spe

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https://doi.org/10.1128/aac.45.5.1522-1527.2001

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A novel hydrophobic diheme c -type cytochrome. Purification from Corynebacterium glutamicum and analysis of the QcrCBA operon encoding three subunit proteins of a putative cytochrome reductase complex 1The nucleotide sequences reported in this paper have been submitted to the DDBJ/GenBank/EMBL Data Bank with accession number AB038380. 1

Autor: Kumiko Nagata, Haruka Kojima, Junnichi Tajima, Tomoe Kanamaru, Nobuhito Sone, Yoriko Kodera, Shunnsuke Noguchi, Junshi Sakamoto

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1503:279-290

Electrophoresis of a Corynebacterium glutamicum membrane preparation in the presence of sodium dodecyl sulfate, followed by staining for peroxidase activity (heme staining), showed only one band at about 28 kDa. This 28 kDa protein was purified from

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6ac9f2c21d8aeedc0644fd2e91e1ac5
https://doi.org/10.1016/s0005-2728(00)00205-x

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Active site structure of SoxB-type cytochrome bo3 oxidase from thermophilic Bacillus

Autor: Junshi Sakamoto, Teizo Kitagawa, Nobuhito Sone, Tatsuki Kurokawa, Motonari Tsubaki, Hiroshi Hori, Takeshi Uchida

Publikováno v: Journal of Inorganic Biochemistry. 82:65-72

Two-subunit SoxB-type cytochrome c oxidase in Bacillus stearothermophilus was over-produced, purified, and examined for its active site structures by electron paramagnetic resonance (EPR) and resonance Raman (RR) spectroscopies. This is cytochrome bo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32749af6160946e1258865c9fc9cff4f
https://doi.org/10.1016/s0162-0134(00)00145-8

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Purification and Characterization of Cytochrome c-553 from Helicobacter pylori

Autor: Shuuji Koyanagi, Sakura Tsukita, Toshihide Tamura, Kumiko Nagata, Nobuhito Sone

Publikováno v: Journal of Biochemistry. 128:371-375

Helicobacter pylori, a microaerophilic Gram-negative spiral bacterium residing in the human stomach, contains a small size soluble cytochrome c. This cytochrome c was purified from the soluble fraction of H. pylori by conventional chromatographies in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e00136b3d01794a12949c23b809fca00
https://doi.org/10.1093/oxfordjournals.jbchem.a022763

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