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

Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift › Peer review

Sammanfattning

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.

Originalspråk	engelska
Sidor (från-till)	149-156
Tidskrift	BBA - Protein Structure and Molecular Enzymology
Volym	1385
Nummer	1
DOI	https://doi.org/10.1016/S0167-4838(98)00035-1
Status	Published - 1998

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10.1016/S0167-4838(98)00035-1

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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.",

keywords = "Dehydrogenase, Channelling, Enzyme kinetics",

author = "{Martinez Arias}, Wilma and Henrik Pettersson and G{\"o}sta Pettersson",

year = "1998",

doi = "10.1016/S0167-4838(98)00035-1",

language = "English",

volume = "1385",

pages = "149--156",

journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",

issn = "1570-9639",

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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

VL - 1385

SP - 149

EP - 156

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -

Mechanism of NADH transfer among dehydrogenases

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