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O Y Dmitriev

Explore the profile of O Y Dmitriev including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 8
Citations 128
Followers 0
Related Specialties
Biochemistry
Biology
Biophysics
Co-Authors
R H Fillingame
W Jiang
P C Jones
K Altendorf
F I Valiyaveetil
Y Zhang
J Hermolin
Published In
Biochim Biophys Acta
J Biol Chem
Eur J Biochem
Proc Natl Acad Sci U S A
J Exp Biol
Affiliations
Soon will be listed here.
Recent Articles
1.
The oligomeric subunit C rotor in the fo sector of ATP synthase: unresolved questions in our understanding of function
Fillingame R, Jiang W, Dmitriev O
J Bioenerg Biomembr . 2004 Jul; 32(5):433-9. PMID: 15254378
We have proposed a model for the oligomeric c-rotor of the F(o) sector of ATP synthase and its interaction with subunit a during H+-transport driven rotation. The model is based...
2.
Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices
Dmitriev O, Fillingame R
J Biol Chem . 2001 May; 276(29):27449-54. PMID: 11331283
The structure of the A20P/P64A mutated subunit c of Escherichia coli ATP synthase, in which the essential proline has been switched from residue 64 of the second transmembrane helix (TMH)...
3.
Structural interpretations of F(0) rotary function in the Escherichia coli F(1)F(0) ATP synthase
Fillingame R, Jiang W, Dmitriev O, Jones P
Biochim Biophys Acta . 2000 Jun; 1458(2-3):387-403. PMID: 10838053
F(1)F(0) ATP synthases are known to synthesize ATP by rotary catalysis in the F(1) sector of the enzyme. Proton translocation through the F(0) membrane sector is now proposed to drive...
4.
Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor
Fillingame R, Jiang W, Dmitriev O
J Exp Biol . 1999 Dec; 203(Pt 1):9-17. PMID: 10600668
H(+)-transporting F(1)F(o)-type ATP synthases utilize a transmembrane H(+) potential to drive ATP formation by a rotary catalytic mechanism. ATP is formed in alternating beta subunits of the extramembranous F(1) sector...
5.
Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme
Dmitriev O, Jones P, Fillingame R
Proc Natl Acad Sci U S A . 1999 Jul; 96(14):7785-90. PMID: 10393899
The structure of the subunit c oligomer of the H+-transporting ATP synthase of Escherichia coli has been modeled by molecular dynamics and energy minimization calculations from the solution structure of...
6.
Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase
Hermolin J, Dmitriev O, Zhang Y, Fillingame R
J Biol Chem . 1999 Jun; 274(24):17011-6. PMID: 10358051
We have previously shown that the E31C-substituted epsilon subunit of F1 can be cross-linked by disulfide bond formation to the Q42C-substituted c subunit of F0 in the Escherichia coli F1F0-ATP...
7.
Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase
Fillingame R, Jones P, Jiang W, Valiyaveetil F, Dmitriev O
Biochim Biophys Acta . 1998 Aug; 1365(1-2):135-42. PMID: 9693732
In this review, we summarize recent work from our laboratory which establishes the topology and nearest neighbor organization of subunits in the F0 sector of the H+ transporting ATP synthase...
8.
Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent
Dmitriev O, Altendorf K, Fillingame R
Eur J Biochem . 1995 Oct; 233(2):478-83. PMID: 7588791
Subunit c of the Escherichia coli F1F0-ATPase, purified in chloroform/methanol (2:1), was reconstituted with detergent-solubilized F0 subunits a and b to form a functionally active H+ channel. The rates of...