Transhydrogenase coupling proton translocation and hydride transfer
نویسندگان
چکیده
منابع مشابه
Development of a Potential Surface for Simulation of Proton and Hydride Transfer Reactions in Solution: Application to NADH Hydride Transfer
This paper presents a new augmented molecular mechanical potential that incorporates significant quantum mechanical effects for proton and hydride transfer reactions in solution and in enzymes. The solvent is treated explicitly, specified covalent bonds in the solute are allowed to break and form, and the charge distribution of the solute is allowed to vary smoothly from that of the reactant to...
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The nicotinamide nucleotide transhydrogenase (TH) is an integral membrane enzyme that uses the proton-motive force to drive hydride transfer from NADH to NADP+ in bacteria and eukaryotes. Here we solved a 2.2-Å crystal structure of the TH transmembrane domain (Thermus thermophilus) at pH 6.5. This structure exhibits conformational changes of helix positions from a previous structure solved at p...
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The gas phase reactivity of 1,3,5-triazine with several oxyanions and carbanions, as well as amide, was evaluated using a flowing afterglow-selected ion flow tube mass spectrometer. Isotopic labeling, H/D exchange, and collision induced dissociation experiments were conducted to facilitate the interpretation of structures and fragmentation processes. A multi-step (→ HCN + HC(2)N ...
متن کاملThe heterotrimer of the membrane-peripheral components of transhydrogenase and the alternating-site mechanism of proton translocation.
Transhydrogenase undergoes conformational changes to couple the redox reaction between NAD(H) and NADP(H) to proton translocation across a membrane. The protein comprises three components: dI, which binds NAD(H); dIII, which binds NADP(H); and dII, which spans the membrane. Experiments using isothermal titration calorimetry, analytical ultracentrifugation, and small angle x-ray scattering show ...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations and Advances
سال: 2014
ISSN: 2053-2733
DOI: 10.1107/s2053273314085040