Mechanism of NADH transfer among dehydrogenases

Wilma Martinez Arias; Henrik Pettersson; Gösta Pettersson

doi:10.1016/S0167-4838(98)00035-1

Mechanism of NADH transfer among dehydrogenases

Wilma Martinez Arias, Henrik Pettersson, Gösta Pettersson

Research output: Contribution to journal › Article › peer-review

Abstract

Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.

Original language	English
Pages (from-to)	149-156
Journal	BBA - Protein Structure and Molecular Enzymology
Volume	1385
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4838(98)00035-1
Publication status	Published - 1998

Subject classification (UKÄ)

Basic Medicine

Free keywords

Dehydrogenase
Channelling
Enzyme kinetics

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10.1016/S0167-4838(98)00035-1

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Cite this

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title = "Mechanism of NADH transfer among dehydrogenases",

abstract = "Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.",

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T1 - Mechanism of NADH transfer among dehydrogenases

AU - Martinez Arias, Wilma

AU - Pettersson, Henrik

AU - Pettersson, Gösta

PY - 1998

Y1 - 1998

N2 - Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.

AB - Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.

KW - Dehydrogenase

KW - Channelling

KW - Enzyme kinetics

U2 - 10.1016/S0167-4838(98)00035-1

DO - 10.1016/S0167-4838(98)00035-1

M3 - Article

SN - 0167-4838

VL - 1385

SP - 149

EP - 156

JO - BBA - Protein Structure and Molecular Enzymology

JF - BBA - Protein Structure and Molecular Enzymology

IS - 1

ER -

Mechanism of NADH transfer among dehydrogenases

Abstract

Subject classification (UKÄ)

Free keywords

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