Online citations, reference lists, and bibliographies.
Please confirm you are human
(Sign Up for free to never see this)
← Back to Search

Effects Of Guanidinium Ions On The Conformational Structure Of Glucose Oxidase Studied By Electrochemistry, Spectroscopy, And Theoretical Calculations: Towards Developing A Chemical-induced Protein Conformation Assay.

Xiaoqing Xu, P. Wu, W. Xu, Qian Shao, L. An, H. Zhang, Chenxin Cai, B. Zhao
Published 2012 · Chemistry, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy
Share
Understanding conformation transitions of proteins in the presence of a chemical denaturant is a topic of great interest because the rich information contained in chemical unfolding is of fundamental importance for proteomic and pharmaceutical research. In this work, the conformational structure changes of glucose oxidase (GOx) induced by guanidinium ions (Gdm(+)) were studied in detail by a combination of electrochemical methods, various spectroscopic techniques including ultraviolet-visible (UV-vis) absorption, fluorescence, Fourier transform infrared (FTIR), and circular dichroism (CD) spectroscopy, molecular dynamics (MD) simulations, and density functional theory (DFT) calculations with the purpose of revealing the mechanism of chemical unfolding of proteins. The results indicated that GOx underwent substantial conformational changes both at the secondary and tertiary structure levels after interacting with Gdm(+) ions. The interaction of GOx with the chemical denaturant resulted in a disturbance of the structure of the flavin prosthetic group (FAD moiety) that induced the moiety to become less exposed to solvent than that in the native protein molecule. The calculation from quantitative second-derivative infrared and CD spectra showed that Gdm(+) ions induced the conversion of α-helix to β-sheet structures. MD simulations and DFT calculations revealed that Gdm(+) ions could enter the active pocket of the GOx molecule and interact with the FAD group, leading to a significant alteration in the structural characteristics and hydrogen bond networks formed between FAD and the surrounding amino acid residues. These alterations in the conformational structure of GOx resulted in a significant decrease in the catalytic activity of the enzyme to glucose oxidation. The study essentially provides an effective way for investigating the mechanism of chemical denaturant-induced protein unfolding, and this approach can be used for assessing the effect of drug molecules on proteins.
This paper references
10.1016/0079-6107(84)90007-5
Hydrogen bonding in globular proteins.
E. Baker (1984)
10.1006/JMBI.1997.1409
Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding.
R. Staniforth (1998)
10.1021/ja903478s
Preferential interactions of guanidinum ions with aromatic groups over aliphatic groups.
Philip E. Mason (2009)
10.1021/ac9015215
Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes.
Xianchan Li (2009)
10.1110/ps.ps.20801
Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein processes and changes in water‐accessible surface area
E. S. Courtenay (2001)
10.1021/jp8112232
Specificity of ion-protein interactions: complementary and competitive effects of tetrapropylammonium, guanidinium, sulfate, and chloride ions.
Philip E. Mason (2009)
10.1093/PROTEIN/5.3.191
Quantitative analysis of protein far UV circular dichroism spectra by neural networks.
G. Boehm (1992)
10.1002/anie.201101016
Cyano groups as probes of protein microenvironments and dynamics.
J. Zimmermann (2011)
10.1074/JBC.273.9.4831
Forcing Thermodynamically Unfolded Proteins to Fold*
I. Baskakov (1998)
10.1021/jp101082d
Contributions of components in guanidine hydrochloride to hemoglobin unfolding investigated by protein film electrochemistry.
Zhibin Mai (2010)
10.1021/ac901005p
Nonenzymatic electrochemical detection of glucose based on palladium-single-walled carbon nanotube hybrid nanostructures.
Ling Meng (2009)
10.1021/jp202640b
Molecular insight into conformational transition of amyloid β-peptide 42 inhibited by (-)-epigallocatechin-3-gallate probed by molecular simulations.
Fu-feng Liu (2011)
10.1073/pnas.0735920100
The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in aqueous solution
P. E. Mason (2003)
10.1021/jp203344u
Electrochemical and spectroscopic studies on the conformational structure of hemoglobin assembled on gold nanoparticles.
Q. Shao (2011)
10.1021/JA067723O
Water penetration into protein secondary structure revealed by hydrogen-deuterium exchange two-dimensional infrared spectroscopy.
L. Deflores (2006)
10.1073/pnas.0708193105
Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15–28 fragment of the Alzheimer amyloid-β protein
A. Baumketner (2008)
10.1149/1.2096541
On the Adsorption of Glucose Oxidase at a Gold Electrode
A. Szucs (1989)
10.1021/LA062064E
pH-dependent protein conformational changes in albumin:gold nanoparticle bioconjugates: a spectroscopic study.
L. Shang (2007)
10.1021/ja208019p
Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.
M. M. Malabanan (2011)
10.1016/J.FOODHYD.2008.03.013
Heat-induced gel formation of plasma proteins: New insights by FTIR 2D correlation spectroscopy
E. Saguer (2009)
10.1021/JA026014H
How ions affect the structure of water.
B. Hribar (2002)
10.1038/nature05695
Atomic structures of amyloid cross-β spines reveal varied steric zippers
M. Sawaya (2007)
10.1038/416483a
Medicine: Danger — misfolding proteins
R. J. Ellis (2002)
10.1006/JMBI.1993.1015
Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution.
H. J. Hecht (1993)
10.1016/J.JMB.2004.10.036
Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains.
A. Möglich (2005)
10.1021/ac1018028
Quantitation, visualization, and monitoring of conformational transitions of human serum albumin by a tetraphenylethene derivative with aggregation-induced emission characteristics.
Yuning Hong (2010)
10.1111/J.1432-1033.2004.04096.X
Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding.
M. K. Santra (2004)
10.1093/jb/mvp029
Guanidine hydrochloride- and urea-induced unfolding of Toxoplasma gondii ferredoxin-NADP+ reductase: stabilization of a functionally inactive holo-intermediate.
K. Singh (2009)
10.1021/ja202849a
Effect of urea on the β-hairpin conformational ensemble and protein denaturation mechanism.
Anna Berteotti (2011)
10.1110/ps.041162705
Modulation of cooperativity in Mycobacterium tuberculosis NADPH‐ferredoxin reductase: Cation‐and pH‐induced alterations in native conformation and destabilization of the NADP+‐binding domain
A. Bhatt (2005)
10.1016/0005-2795(69)90014-2
The relationship between molecular conformation and the binding of flavin-adenine dinucleotide in glucose oxidase.
B. Swoboda (1969)
10.1021/AC020103V
Single-pass attenuated total reflection Fourier transform infrared spectroscopy for the analysis of proteins in H2O solution.
B. Smith (2002)
10.1074/JBC.M208711200
Thermal Inactivation of Glucose Oxidase
M. D. Gouda (2003)
10.1021/ja8031289
Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes.
O. K. Abou-Zied (2008)
10.1073/pnas.091100898
Tryptophan zippers: Stable, monomeric β-hairpins
A. Cochran (2001)
10.1146/ANNUREV.BIOCHEM.66.1.385
Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins.
J. Harper (1997)
10.1021/la901885d
Probing the conformation and orientation of adsorbed enzymes using side-chain modification.
K. Fears (2009)
10.1021/jp8097318
Measurement of DNA morphological parameters at highly entangled regime on surfaces.
A. Calò (2009)
10.1016/J.JCIS.2005.01.071
Stabilizing effect of low concentrations of urea on reverse micelles.
A. Chakraborty (2005)
10.1021/la200376f
Effect of low molecular weight additives on immobilization strength, activity, and conformation of protein immobilized on PVC and UHMWPE.
A. Kondyurin (2011)
10.1021/bi201526y
Protein conformational changes of the oxidative stress sensor, SoxR, upon redox changes of the [2Fe-2S] cluster probed with ultraviolet resonance Raman spectroscopy.
K. Kobayashi (2011)
10.1021/JA0761939
Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.
Troy Cellmer (2007)
10.1038/75151
Two exposed amino acid residues confer thermostability on a cold shock protein
Dieter Perl (2000)
10.1021/BM049744L
Effect of colloidal gold size on the conformational changes of adsorbed cytochrome c: probing by circular dichroism, UV-visible, and infrared spectroscopy.
X. Jiang (2005)
10.1021/jp106214v
New insights into the effects of thermal treatment on the catalytic activity and conformational structure of glucose oxidase studied by electrochemistry, IR spectroscopy, and theoretical calculation.
Q. Wang (2010)
10.1021/BI020080E
Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer.
M. S. Akhtar (2002)
10.1021/jp904475v
Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids.
Taylor A Page (2009)
10.1021/jp800913k
Preparation and characterization of a novel electrospun spider silk fibroin/poly(D,L-lactide) composite fiber.
S. Zhou (2008)
10.1016/J.CEJ.2008.11.033
Small-angle neutron scattering studies of model protein denaturation in aqueous solutions of the ionic liquid 1-butyl-3-methylimidazolium chloride
G. A. Baker (2009)
pH-induced changes in activity and conformation of NADH oxidase from Thermus thermophilus.
G. Žoldák (2005)
10.1021/BI992271W
Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface.
V. Loladze (1999)
10.1021/JP010714B
Monolayers of Apolipoproteins at the Air/Water Interface
V. Bolanos-Garcia (2001)
10.1021/JP0674874
Two-dimensional infrared spectral signatures of 310-and α-helical peptides
H. Maekawa (2007)
10.1021/jp1054342
Effect of association with sulfate on the electrophoretic mobility of polyarginine and polylysine.
E. Wernersson (2010)
10.1016/S0022-2836(05)80179-2
Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger.
H. Kalisz (1990)
10.1021/jp904001m
Effects of urea and trimethylamine-N-oxide on the properties of water and the secondary structure of hen egg white lysozyme.
A. Panuszko (2009)
10.1021/LA062916A
Diazonium-functionalized horseradish peroxidase immobilized via addressable electrodeposition: direct electron transfer and electrochemical detection.
R. Polsky (2007)
10.1021/PR0501968
Characterization of local polarity and hydrophobic binding sites of beta-lactoglobulin by using N-terminal specific fluorescence labeling.
Su-Ying Dong (2006)
10.1021/bi9020082
Preferential interactions between small solutes and the protein backbone: a computational analysis.
Liang Ma (2010)
10.1021/BI001933A
Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
A. Ahmad (2001)
10.1073/pnas.0606236103
A molecular mechanism for osmolyte-induced protein stability
Timothy O. Street (2006)
10.1042/BJ20041296
Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy.
A. Natalello (2005)
10.1021/ac902442g
Tissue phantoms constructed with hydrophobic nanoporous silica particles.
Yulia A. Skvortsova (2010)
10.1021/BI0359325
Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence.
O. Stepanenko (2004)
10.1021/ac802421h
Detection of glucose based on direct electron transfer reaction of glucose oxidase immobilized on highly ordered polyaniline nanotubes.
Ziyi Wang (2009)
10.1021/ja201349g
Complex ion effects on polypeptide conformational stability: chloride and sulfate salts of guanidinium and tetrapropylammonium.
C. Dempsey (2011)
10.1016/S0959-440X(98)80101-2
Conformational changes and disease--serpins, prions and Alzheimer's.
R. Carrell (1998)
10.1021/jp2071925
New insight into molecular interactions of imidazolium ionic liquids with bovine serum albumin.
Y. Shu (2011)
10.1074/jbc.274.16.10693
Trimethylamine N-Oxide-induced Cooperative Folding of an Intrinsically Unfolded Transcription-activating Fragment of Human Glucocorticoid Receptor*
I. Baskakov (1999)
10.1021/jp905632k
Effects of ionic liquids on enzymatic catalysis of the glucose oxidase toward the oxidation of glucose.
Xiuming Wu (2009)
10.1021/MA101862B
Amperometric Detection of Glucose Using a Conjugated Polyelectrolyte Complex with Single-Walled Carbon Nanotubes
X. Pang (2010)
10.1021/BI992091M
Rational modification of protein stability by the mutation of charged surface residues.
Steven Spector (2000)
10.1529/BIOPHYSJ.105.066142
Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation.
H. He (2005)
10.1021/jp9002356
Temperature and chemical denaturant dependence of forced unfolding of titin I27.
E. Botello (2009)
10.1073/PNAS.92.12.5553
Sticky ions in biological systems.
K. Collins (1995)
10.1016/S0079-6107(99)00007-3
Structure and dynamics of membrane proteins as studied by infrared spectroscopy.
J. L. Arrondo (1999)
10.1529/BIOPHYSJ.107.108290
The interaction of guanidinium ions with a model peptide.
Philip E. Mason (2007)
10.1021/LA063627P
Silver-protein (core-shell) nanoparticle production using spent mushroom substrate.
N. Vigneshwaran (2007)
10.1038/nature02261
Protein folding and misfolding
C. Dobson (2003)
10.1016/j.colsurfb.2009.05.008
The formation of pepsin monomolecular layer by the Langmuir-Blodgett film deposition technique.
Prabir Pal (2009)
10.1021/BI960341I
Guanidine Hydrochloride Unfolding of Peptide Helices: Separation of Denaturant and Salt Effects†
Smith Js (1996)
10.1021/ja8089476
Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
Sanne M. Nabuurs (2009)
10.1016/S1381-1177(99)00030-2
FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
P. Haris (1999)
10.1021/JP0473218
A theoretical investigation of the shape and hydration properties of aqueous urea: Evidence for nonplanar urea geometry
T. Ishida (2004)



This paper is referenced by
10.1039/c3cp52352g
Electrochemical probing of the solution pH-induced structural alterations around the heme group in myoglobin.
Yingdan Qian (2013)
10.1016/j.ijbiomac.2018.03.083
The influence of two imidazolium-based ionic liquids on the structure and activity of glucose oxidase: Experimental and theoretical studies.
F. Janati-Fard (2018)
10.1016/j.jelechem.2019.113472
Modulating the electron transport energy levels of protein by doping with foreign molecule
Wenhui Liang (2019)
10.1016/j.colsurfb.2013.03.033
Graphene oxide-induced conformation changes of glucose oxidase studied by infrared spectroscopy.
Q. Shao (2013)
10.1016/J.SNB.2016.07.138
The impact of immobilization process on the electrochemical performance, bioactivity and conformation of glucose oxidase enzyme
Barbara Kowalewska (2017)
10.1016/j.msec.2015.05.038
Improvement in glucose biosensing response of electrochemically grown polypyrrole nanotubes by incorporating crosslinked glucose oxidase.
Pragya Agar Palod (2015)
10.1016/J.MOLCATB.2016.09.008
Investigation of structural stability and enzymatic activity of glucose oxidase and its subunits
F. Janati-Fard (2016)
10.1039/c2cp40654c
Insight into the effects of graphene oxide sheets on the conformation and activity of glucose oxidase: towards developing a nanomaterial-based protein conformation assay.
Q. Shao (2012)
10.1016/j.ijbiomac.2017.08.018
How a multimeric macromolecule is affected by divalent salts? Experimental and simulation study.
F. Janati-Fard (2018)
10.1016/j.jcis.2014.12.033
Probing the anticancer-drug-binding-induced microenvironment alterations in subdomain IIA of human serum albumin.
X. Xu (2015)
10.1039/c9cc00688e
Tuning the electron transport band gap of bovine serum albumin by doping with Vb12.
Wenhui Liang (2019)
10.1016/j.foodchem.2019.124981
Nanomolar level sensing of glucose in food samples using glucose oxidase confined MWCNT-Inulin-TiO2 bio-nanocomposite.
G. Jayanthi Kalaivani (2019)
10.1016/J.ELECTACTA.2015.01.114
Conformation, Bioactivity and Electrochemical Performance of Glucose Oxidase Immobilized on Surface of Gold Nanoparticles
Yonghai Song (2015)
10.1021/jp506429a
Hydration of guanidinium: second shell formation at small cluster size.
R. J. Cooper (2014)
Semantic Scholar Logo Some data provided by SemanticScholar