Enhanced supply of acetyl-CoA by exogenous pantothenate kinase promotes synthesis of poly(3-hydroxybutyrate)

Autor: Hirotaka Kudo, Sho Ono, Kenta Abe, Mami Matsuda, Tomohisa Hasunuma, Tomoyasu Nishizawa, Munehiko Asayama, Hirofumi Nishihara, Shigeru Chohnan

Publikováno v: Microbial Cell Factories, Vol 22, Iss 1, Pp 1-13 (2023)

Abstract Background Coenzyme A (CoA) is a carrier of acyl groups. This cofactor is synthesized from pantothenic acid in five steps. The phosphorylation of pantothenate is catalyzed by pantothenate kinase (CoaA), which is a key step in the CoA biosynt

Externí odkaz: https://doaj.org/article/5375cfa8eb5c4f3d86d31981d33055bc

Structural and functional insights into thermally stable cytochromec′ from a thermophile

Autor: Yoshihiro Sambongi, Takahiro Maruno, Daisuke Yamane, Tadayasu Ohkubo, Hirofumi Nishihara, Yuji Kobayashi, Sotaro Fujii, Hiroya Oki, Masaru Yamanaka, Misa Masanari, Satoshi Wakai, Kazuki Kawahara

Publikováno v: Protein Science. 26:737-748

This work was performed under the Cooperative Research Program of the “Network Joint Research Center for Materials and Devices”.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c3437dfdd067eff44ca9760667f3dc5a
https://doi.org/10.1002/pro.3120

Improved purification, crystallization and crystallographic study of Hyd-2-type [NiFe]-hydrogenase fromCitrobactersp. S-77

Autor: Hirofumi Nishihara, Noor Dina Muhd Noor, Seiji Ogo, Ki Seok Yoon, Yoshiki Higuchi, Koji Nishikawa

Publikováno v: Acta Crystallographica Section F Structural Biology Communications. 72:53-58

The purification procedure of Hyd-2-type [NiFe]-hydrogenase fromCitrobactersp. S-77 was improved by applying treatment with trypsin before chromatography. Purified protein samples both with and without trypsin treatment were successfully crystallized

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b281b7756b4f9e01ff07fb145dbe7704
https://doi.org/10.1107/s2053230x15024152

Structural differences of oxidized iron–sulfur and nickel–iron cofactors in O2-tolerant and O2-sensitive hydrogenases studied by X-ray absorption spectroscopy

Autor: Oliver Lenz, Hirofumi Nishihara, Petko Chernev, Fraser A. Armstrong, Nils Leidel, Kajsa G.V. Sigfridsson, Marc Rousset, Antonio L. De Lacey, Ki Seok Yoon, Oliver Sanganas, Michael Haumann, Sébastien Dementin, Alison Parkin

Publikováno v: Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2015, 1847 (2), pp.162-170. ⟨10.1016/j.bbabio.2014.06.011⟩
Digital.CSIC. Repositorio Institucional del CSIC
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Biochimica biophysica acta (BBA)-Bioenergetics, 2015, 1847 (2), pp.162-170. ⟨10.1016/j.bbabio.2014.06.011⟩

The class of [NiFe]-hydrogenases comprises oxygen-sensitive periplasmic (PH) and oxygen-tolerant membrane-bound (MBH) enzymes. For three PHs and four MBHs from six bacterial species, structural features of the nickel–iron active site of hydrogen tu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8703f353ab83acb29b8d528d3aebaa72

Oxidative phosphorylation in a thermophilic, facultative chemoautotroph,Hydrogenophilus thermoluteolus, living prevalently in geothermal niches

Autor: Kaori Watanabe, Satoshi Wakai, Yoshihiro Sambongi, Saori Ueshima, Hirofumi Nishihara, Naho Yamaguchi, Misa Masanari, Takumi Ikeda

Publikováno v: Environmental Microbiology Reports. 5:235-242

Summary Hydrogenophilus is a thermophilic, facultative chemoautotroph, which lives prevalently in high temperature geothermal niches. Despite the environmental distribution, little is known about its oxidative phosphorylation. Here, we show that inve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5890cc18be999c05c7bcb88176a63f53
https://doi.org/10.1111/1758-2229.12005