Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase

Emel B. Ordu; Gus Cameron; Anthony R. Clarke; Nevin Gül Karagüler

doi:10.1016/j.febslet.2009.07.048

Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase

Emel B. Ordu
, Gus Cameron
, Anthony R. Clarke
, Nevin Gül Karagüler^*

^*Bu çalışma için yazışmadan sorumlu yazar

Mol.Biyoloji ve Genetik Bölümü

Istanbul Technical University
Yildiz Technical University
University of Bristol

Araştırma sonucu: Dergiye katkı › Makale › bilirkişi

10 Atıf (Scopus)

Özet

The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10^-13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k₁) of about 2 × 10^-3 s^-1 (by deduction k_-1 is about10^-4 s^-1) and assembles into the active dimeric state with a bimolecular rate constant (k₂) of about 2 × 10⁴ M^-1 s^-1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k_-2 ∼ 3 × 10^-7 s^-1).

Orijinal dil	İngilizce
Sayfa (başlangıç-bitiş)	2887-2892
Sayfa sayısı	6
Dergi	FEBS Letters
Hacim	583
Basın numarası	17
DOI'lar	https://doi.org/10.1016/j.febslet.2009.07.048
Yayın durumu	Yayınlandı - 3 Eyl 2009

Finansman

This work was partially supported by the Turkish State Planning Organization’s Advanced Technologies Program and Turkish State Planning Organization (Project No. 90188).

Finansörler	Finansör numarası
Turkish State Planning Organization	90188

Belgeye Erişim

10.1016/j.febslet.2009.07.048

Diğer Dosyalar ve Linkler

Link to publication in Scopus

Alıntı Yap

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title = "Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase",

abstract = "The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10-13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k1) of about 2 × 10-3 s-1 (by deduction k-1 is about10-4 s-1) and assembles into the active dimeric state with a bimolecular rate constant (k2) of about 2 × 104 M-1 s-1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k-2 ∼ 3 × 10-7 s-1).",

keywords = "Assembly mechanism, Candida methylica, Folding mechanism, Formate dehydrogenase",

author = "Ordu, \{Emel B.\} and Gus Cameron and Clarke, \{Anthony R.\} and Karag{\"u}ler, \{Nevin G{\"u}l\}",

year = "2009",

month = sep,

day = "3",

doi = "10.1016/j.febslet.2009.07.048",

language = "English",

volume = "583",

pages = "2887--2892",

journal = "FEBS Letters",

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TY - JOUR

T1 - Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase

AU - Ordu, Emel B.

AU - Cameron, Gus

AU - Clarke, Anthony R.

AU - Karagüler, Nevin Gül

PY - 2009/9/3

Y1 - 2009/9/3

N2 - The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10-13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k1) of about 2 × 10-3 s-1 (by deduction k-1 is about10-4 s-1) and assembles into the active dimeric state with a bimolecular rate constant (k2) of about 2 × 104 M-1 s-1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k-2 ∼ 3 × 10-7 s-1).

AB - The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10-13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k1) of about 2 × 10-3 s-1 (by deduction k-1 is about10-4 s-1) and assembles into the active dimeric state with a bimolecular rate constant (k2) of about 2 × 104 M-1 s-1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k-2 ∼ 3 × 10-7 s-1).

KW - Assembly mechanism

KW - Candida methylica

KW - Folding mechanism

KW - Formate dehydrogenase

UR - https://www.scopus.com/pages/publications/69249208701

U2 - 10.1016/j.febslet.2009.07.048

DO - 10.1016/j.febslet.2009.07.048

M3 - Article

C2 - 19647736

AN - SCOPUS:69249208701

SN - 0014-5793

VL - 583

SP - 2887

EP - 2892

JO - FEBS Letters

JF - FEBS Letters

IS - 17

ER -

Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase

Özet

Finansman

Belgeye Erişim

Diğer Dosyalar ve Linkler

Parmak izi

Alıntı Yap