[NMR paper] Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure
Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure
Proton translocation through the membrane-embedded F(o) component of F-type ATP synthase (F(o)F(1)) is facilitated by the rotation of the F(o) c-subunit ring (c-ring), carrying protons at essential acidic amino acid residues. Cryo-electron microscopy (Cryo-EM) structures of F(o)F(1) suggest a unique proton translocation mechanism. To elucidate it based on the chemical conformation of the essential acidic residues of the c-ring in F(o)F(1), we determined the structure of the isolated thermophilic...
[NMR paper] Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
J Biomol NMR. 2017 Dec 02;:
Authors: Kang SJ, Todokoro Y, Bak S, Suzuki T, Yoshida M, Fujiwara T, Akutsu H
Abstract
FoF1-ATP synthase catalyzes ATP hydrolysis/synthesis coupled with a transmembrane H+ translocation in membranes. The Fo...
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12-05-2017 07:35 PM
Direct assignment of 13 C solid-state NMR signals of TF o F 1 ATP synthase subunit c -ring in lipid membranes and its implication for the ring structure
Direct assignment of 13 C solid-state NMR signals of TF o F 1 ATP synthase subunit c -ring in lipid membranes and its implication for the ring structure
Abstract
FoF1-ATP synthase catalyzes ATP hydrolysis/synthesis coupled with a transmembrane H+ translocation in membranes. The Fo c-subunit ring plays a major role in this reaction. We have developed an assignment strategy for solid-state 13C NMR (ssNMR) signals of the Fo c-subunit ring of thermophilic Bacillus PS3 (TFo ...
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12-03-2017 04:52 AM
[NMR paper] Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Active-site structure of the thermophilic foc-subunit ring in membranes elucidated by solid-state NMR.
Biophys J. 2014 Jan 21;106(2):390-8
Authors: Kang SJ, Todokoro Y, Yumen I, Shen B, Iwasaki I, Suzuki T, Miyagi A, Yoshida M, Fujiwara T, Akutsu H
Abstract
FoF1-ATP synthase uses the electrochemical potential across membranes or ATP hydrolysis to rotate the Foc-subunit ring. To elucidate the underlying mechanism, we carried out a...
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01-28-2014 11:53 AM
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
J Biomol NMR. 2010 Sep;48(1):1-11
Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H
The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
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12-18-2010 12:00 PM
[NMR paper] Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase reveal
Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
Related Articles Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 15;127(23):8424-32
Authors: Wu J, Bell AF, Jaye AA, Tonge PJ
Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. The interaction of hexadienoyl-CoA (HD-CoA), a product analogue, with recombinant pig...
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11-25-2010 08:21 PM
[NMR paper] Aromatic ring-flipping in supercooled water: implications for NMR-based structural bi
Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
Related Articles Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
J Am Chem Soc. 2001 Jan 24;123(3):388-97
Authors: Skalicky JJ, Mills JL, Sharma S, Szyperski T
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at...
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11-19-2010 08:32 PM
[NMR paper] Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by so
Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.
Related Articles Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.
Biochemistry. 1992 Oct 27;31(42):10390-9
Authors: Ulrich AS, Heyn MP, Watts A
The orientation and conformation of retinal within bacteriorhodopsin of the purple membrane of Halobacterium halobium was established by solid-state deuterium NMR spectroscopy, through the determination of individual chemical bond...