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2017年03月17日 掲載 (Published 03/17/2017)


「Biophysics and Physicobiology」にNoriyo Mitome et al. “Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the F o- a subunit of Propionigenium modestum ATP synthase”を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Noriyo Mitome, Hiroki Sato, Taishi Tomiyama,Katsuya Shimabukuro,
Takuya Matsunishi, Kohei Hamada,Toshiharu Suzuki
“Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo- a subunit of Propionigenium modestum ATP synthase”

【Significance】
Aqueous access residues in P. modestum Na+ F-ATPase

The Fo- a subunit of the Na+-transporting FoF1 ATP synthase from Propionigenium modestum has an important role in Na+ transport. To clarify the role of amino-acid residues of transmembrane helix 5 in this subunit, 25 residues were individually mutated to Cys and effects of SH-modification with N-ethylmaleimide (NEM) on ATP synthesis and hydrolysis activity were analyzed. ATP synthesis and hydrolysis and proton pumping activities of A214C, G215C, A218C, I223C and N230C mutants and ATP synthesis activity of the K219C mutant were inhibited. Thus, these residues contribute to the Na+ half-channel integrity; both half channels are present in the F o- a subunit.

Biophysics and Physicobiology, Vol.14, pp. 41-47

URL:https://www.jstage.jst.go.jp/article/biophysico/14/0/14_41/_article