Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel

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Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel. / Jackson, John; Leung, Josephine H.; Stout, Charles D.; Schurig-briccio, Lici A.; Gennis, Robert B.

In: FEBS Letters, Vol. 589, No. 16, 01.07.2015, p. 2027-2033.

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Jackson, John ; Leung, Josephine H. ; Stout, Charles D. ; Schurig-briccio, Lici A. ; Gennis, Robert B. / Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel. In: FEBS Letters. 2015 ; Vol. 589, No. 16. pp. 2027-2033.

Bibtex

@article{e1fbe8d679c14c4abc6e3f4be9ef5db0,
title = "Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel",
abstract = "The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP+ by NADH to proton translocation. Recent X-ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of the two dIII components of the enzyme dimer (Leung et al., 2015). The character of the orientation change, and a review of information on the kinetics and thermodynamics of transhydrogenase, indicate that dIII swivelling might assist in the control of proton gating by the redox state of bound NADP+/NADPH during enzyme turnover.",
keywords = "Transhydrogenase, Membrane-protein structure, Nicotinamide nucleotide, Proton-pump, Proton-gating",
author = "John Jackson and Leung, {Josephine H.} and Stout, {Charles D.} and Schurig-briccio, {Lici A.} and Gennis, {Robert B.}",
year = "2015",
month = jul,
day = "1",
doi = "10.1016/j.febslet.2015.06.027",
language = "English",
volume = "589",
pages = "2027--2033",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "16",

}

RIS

TY - JOUR

T1 - Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel

AU - Jackson, John

AU - Leung, Josephine H.

AU - Stout, Charles D.

AU - Schurig-briccio, Lici A.

AU - Gennis, Robert B.

PY - 2015/7/1

Y1 - 2015/7/1

N2 - The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP+ by NADH to proton translocation. Recent X-ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of the two dIII components of the enzyme dimer (Leung et al., 2015). The character of the orientation change, and a review of information on the kinetics and thermodynamics of transhydrogenase, indicate that dIII swivelling might assist in the control of proton gating by the redox state of bound NADP+/NADPH during enzyme turnover.

AB - The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP+ by NADH to proton translocation. Recent X-ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of the two dIII components of the enzyme dimer (Leung et al., 2015). The character of the orientation change, and a review of information on the kinetics and thermodynamics of transhydrogenase, indicate that dIII swivelling might assist in the control of proton gating by the redox state of bound NADP+/NADPH during enzyme turnover.

KW - Transhydrogenase

KW - Membrane-protein structure

KW - Nicotinamide nucleotide

KW - Proton-pump

KW - Proton-gating

U2 - 10.1016/j.febslet.2015.06.027

DO - 10.1016/j.febslet.2015.06.027

M3 - Article

VL - 589

SP - 2027

EP - 2033

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 16

ER -