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Electrochemical Probing Of The Solution PH-induced Structural Alterations Around The Heme Group In Myoglobin.

Yingdan Qian, X. Xu, Q. Wang, P. Wu, Hui Bin Zhang, C. Cai
Published 2013 · Chemistry, Medicine

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Protein folding-unfolding has received considerable attention because of its fundamental importance in the manifestation of biological functions, in molecular diagnostics, in drug development, and its close relationship to human health. Although many attempts have been made to study and monitor the protein unfolding, a facile and effective method for probing the structural changes of proteins is still highly desired. This work reports electrochemical voltammetry for probing the structural alterations around the heme group in myoglobin (Mb) induced by solution pH. This approach is based on the changes of the electron transfer (ET) signals of Mb upon the structural alteration because the heme group is deeply buried in the hydrophobic pocket in neutral conditions (in the native state), resulting in poor ET signals, while it dissociates from the hydrophobic pocket and becomes exposed to the solution in acidic and basic conditions (in the unfolding state) due to the breakage of the Fe-His93 bond, causing an obvious enhancement in ET signals. The good consistency of the results obtained with our electrochemical method with those of spectroscopic measurements (such as UV-vis, CD, and Raman spectroscopy) and molecular dynamics (MD) simulations substantially validates that our proposed method is a facile and effective way for probing structural changes around the heme group in Mb. Compared with the existing methods used for the study of structural changes of protein, our method demonstrated here could be advantageous in terms of its sensitivity, ease of operation, cost-effective feature, simple use of bare electrodes, and availability of abundant dynamic information. This study essentially offers a facile and effective electrochemical route to probe the structural changes around the heme group and the conformation alterations of heme-containing proteins.
This paper references
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/BI001933A
Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
A. Ahmad (2001)
10.1021/BI00251A039
Acid-induced transformations of myoglobin. Characterization of a new equilibrium heme-pocket intermediate.
V. Palaniappan (1994)
10.1021/JA00334A024
Confirmation of the assignment of the iron-histidine stretching mode in myoglobin
P. Argade (1984)
10.1021/la903387n
A comparison of the higher order harmonic components derived from large-amplitude Fourier transformed ac voltammetry of myoglobin and heme in DDAB films at a pyrolytic graphite electrode.
Chong-Yong Lee (2010)
10.1016/S0022-0728(99)00142-4
The temperature dependence of the kinetics of cyanide dissociation from the cyanide complex of myoglobin studied by cyclic voltammetry
Lucy Duah-Williams (1999)
10.1021/BI00219A010
Spectroscopic studies of myoglobin at low pH: heme structure and ligation.
J. T. Sage (1991)
10.1021/BI00187A023
Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly.
D. Barrick (1994)
10.1021/jp205770p
Molecular mechanism of the effects of salt and pH on the affinity between protein A and human immunoglobulin G1 revealed by molecular simulations.
Bo Huang (2012)
10.1007/BF02698108
Separation of proteins in a transient ph gradient column
Jae-Young Bae (1989)
10.1038/416483a
Medicine: Danger — misfolding proteins
R. J. Ellis (2002)
10.1074/jbc.M600061200
On the Relationship of Coral Allene Oxide Synthase to Catalase
T. Tosha (2006)
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/la200376f
Effect of low molecular weight additives on immobilization strength, activity, and conformation of protein immobilized on PVC and UHMWPE.
A. Kondyurin (2011)
10.2210/PDB1MBN/PDB
The Stereochemistry of the Protein Myoglobin
H. C. Watson (1976)
10.1039/c2cp24121h
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 (2012)
10.1021/jp203344u
Electrochemical and spectroscopic studies on the conformational structure of hemoglobin assembled on gold nanoparticles.
Q. Shao (2011)
10.1021/la3048278
Design and application of anthracene derivative with aggregation-induced emission charateristics for visualization and monitoring of erythropoietin unfolding.
Binjie Sun (2013)
10.1021/ac303265q
Monitoring guanidinium-induced structural changes in ribonuclease proteins using Raman spectroscopy and 2D correlation analysis.
V. Brewster (2013)
10.1021/JA050321G
Electrochemistry of unfolded cytochrome c in neutral and acidic urea solutions.
M. Fedurco (2005)
10.1006/BBRC.1994.2867
Kinetics of conformation change in cyanometmyoglobin following electron transfer monitored by magnetically induced circular dichroism spectrometry.
K. Nishiyama (1994)
10.1021/LA063627P
Silver-protein (core-shell) nanoparticle production using spent mushroom substrate.
N. Vigneshwaran (2007)
10.1021/AC060351H
Chemical-induced unfolding of cofactor-free protein monitored by electrochemistry.
L. Guo (2006)
10.1021/JP105870Z
In Situ FTIR ATR Spectroscopic Study of the Interaction of Immobilized Human Serum Albumin with Cholate in Aqueous Environment
N. Hassler (2011)
The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid.
D. Puett (1973)
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)
10.1021/jp205094c
Contribution of dynamic and static quenchers for the study of protein conformation in ionic liquids by steady-state fluorescence spectroscopy.
Mourad Bekhouche (2012)
10.5796/kogyobutsurikagaku.63.390
The Unfolding Effects of Urea on the Myoglobin-Imidazole Complex Studied by Cyclic Voltammetry and Visible Absorption Spectroscopy
Percy L. Torkornoo (1995)
10.1016/j.colsurfb.2013.03.033
Graphene oxide-induced conformation changes of glucose oxidase studied by infrared spectroscopy.
Q. Shao (2013)
10.1021/JP305891P
Ultrafast Dynamics of Metal Complexes of Tetrasulfonated Phthalocyanines at Biological Interfaces: Comparison between Photochemistry in Solutions, Films, and Noncancerous and Cancerous Human Breast Tissues
H. Abramczyk (2013)
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)
10.1021/jp905632k
Effects of ionic liquids on enzymatic catalysis of the glucose oxidase toward the oxidation of glucose.
Xiuming Wu (2009)
10.1074/JBC.M208711200
Thermal Inactivation of Glucose Oxidase
M. D. Gouda (2003)
10.1021/AC035416K
Denaturation and renaturation of self-assembled yeast iso-1-cytochrome c on Au.
S. Chah (2004)
10.1038/75151
Two exposed amino acid residues confer thermostability on a cold shock protein
Dieter Perl (2000)
10.1016/J.AB.2004.05.057
Direct electron transfer of glucose oxidase promoted by carbon nanotubes.
Chenxin Cai (2004)
10.1038/nature02261
Protein folding and misfolding
C. Dobson (2003)
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)
10.1021/jp308433a
Ultrafast hydrogen-bonding dynamics in the electronic excited state of photoactive yellow protein revealed by femtosecond stimulated Raman spectroscopy.
R. Nakamura (2012)
10.1134/S0026893306020154
Conformational dynamics of the tetrameric hemoglobin molecule as revealed by hydrogen exchange: I. Effects of pH, temperature, and ligand binding
L. V. Abaturov (2006)
10.1016/J.AB.2003.10.040
Direct electron transfer and bioelectrocatalysis of hemoglobin at a carbon nanotube electrode.
Chenxin Cai (2004)
10.1021/jp9002356
Temperature and chemical denaturant dependence of forced unfolding of titin I27.
E. Botello (2009)
10.1021/ja8049063
High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering.
Jason J Lavinder (2009)
10.1021/la201496j
Headgroup effects of template monolayers on the adsorption behavior and conformation of glucose oxidase adsorbed at air/liquid interfaces.
Ke-hsuan Wang (2011)
10.1021/jp101082d
Contributions of components in guanidine hydrochloride to hemoglobin unfolding investigated by protein film electrochemistry.
Zhibin Mai (2010)
10.1038/nature05695
Atomic structures of amyloid cross-β spines reveal varied steric zippers
M. Sawaya (2007)
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)



This paper is referenced by
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.jinorgbio.2017.04.011
Three phases in pH dependent heme abstraction from myoglobin.
Sohini Mukherjee (2017)
10.1016/j.bioelechem.2017.11.012
Determination of the formal redox potentials of the cyanhaemoglobin/cyanmethaemoglobin and the myoglobin/metmyoglobin couples at neutral pH.
L. Mahmoudi (2018)
10.22175/MMB2017.04.0022
Benchmarking Venezuelan Quality Grades for Grass-Fed Cattle Carcasses
A. Rodas-González (2017)
10.1016/j.jphotobiol.2018.07.007
Binding interaction of phenazinium-based cationic photosensitizers with human hemoglobin: Exploring the effects of pH and chemical structure.
Swagata Sen (2018)
10.1039/C6CP05216A
Contrasting effects of pH on the modulation of the structural integrity of hemoglobin induced by sodium deoxycholate.
Ramakanta Mondal (2016)
10.2116/analsci.33.435
Electron-Transfer Rate in Potential-Modulated Redox Reactions with Electro-Active Optical Waveguides.
Xue Han (2017)
10.1016/J.ELECOM.2014.06.006
A microtubular all CNT gas diffusion electrode
Y. Gendel (2014)
10.1039/c9cc00688e
Tuning the electron transport band gap of bovine serum albumin by doping with Vb12.
Wenhui Liang (2019)
10.1021/acs.analchem.6b00131
Highly Selective Fluorescence Determination of the Hematin Level in Human Erythrocytes with No Need for Separation from Bulk Hemoglobin.
Lijuan Ji (2016)
10.3390/polym10090964
Designing the Slide-Ring Polymer Network with both Good Mechanical and Damping Properties via Molecular Dynamics Simulation
Zhiyu Zhang (2018)
10.22175/MMB2016.10.0003
Species-Specificity in Myoglobin Oxygenation and Reduction Potential Properties
Rajasekhara Nerimetla (2017)
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)
10.1007/s10904-018-0932-6
Investigation on Electrochemical Behavior and Catalytic Function of Glassy Carbon Electrode on the Basis of Magnetic Nano-particle with Simultaneous Incorporation of Myoglobin and Electron Mediator
H. Zeng (2018)
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