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Items: 8

1.

Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-a subunit of Propionigenium modestum ATP synthase.

Mitome N, Sato H, Tomiyama T, Shimabukuro K, Matsunishi T, Hamada K, Suzuki T.

Biophys Physicobiol. 2017 Mar 1;14:41-47. doi: 10.2142/biophysico.14.0_41. eCollection 2017.

2.

Essential arginine residue of the F(o)-a subunit in F(o)F(1)-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F(o) proton channel.

Mitome N, Ono S, Sato H, Suzuki T, Sone N, Yoshida M.

Biochem J. 2010 Aug 15;430(1):171-7. doi: 10.1042/BJ20100621.

PMID:
20518749
3.

[ATP synthase: highly organized molecular structure and its marvelous function].

Hisabori T, Shimabukuro K, Mitome N.

Tanpakushitsu Kakusan Koso. 2005 Aug;50(10 Suppl):1151-9. Review. Japanese. No abstract available.

PMID:
16104579
4.

Thermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling.

Mitome N, Suzuki T, Hayashi S, Yoshida M.

Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12159-64. Epub 2004 Aug 9.

5.

F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring.

Suzuki T, Ueno H, Mitome N, Suzuki J, Yoshida M.

J Biol Chem. 2002 Apr 12;277(15):13281-5. Epub 2002 Jan 28.

6.

The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase.

Mitome N, Ono S, Suzuki T, Shimabukuro K, Muneyuki E, Yoshida M.

Eur J Biochem. 2002 Jan;269(1):53-60.

7.

Second stalk of ATP synthase. Cross-linking of gamma subunit in F1 to truncated Fob subunit prevents ATP hydrolysis.

Suzuki T, Suzuki J, Mitome N, Ueno H, Yoshida M.

J Biol Chem. 2000 Dec 1;275(48):37902-6.

8.

Rotation of F(1)-ATPase and the hinge residues of the beta subunit.

Masaike T, Mitome N, Noji H, Muneyuki E, Yasuda R, Kinosita K, Yoshida M.

J Exp Biol. 2000 Jan;203(Pt 1):1-8. Review.

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