Base de dados : MEDLINE
Pesquisa : D03.383.129.578.840.500.640.587.462 [Categoria DeCS]
Referências encontradas : 3414 [refinar]
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[PMID]:29219496
[Au] Autor:Olafson KN; Rimer JD; Vekilov PG
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, Texas 77204-4004, USA.
[Ti] Título:Early Onset of Kinetic Roughening due to a Finite Step Width in Hematin Crystallization.
[So] Source:Phys Rev Lett;119(19):198101, 2017 Nov 10.
[Is] ISSN:1079-7114
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The structure of the interface of a growing crystal with its nutrient phase largely determines the growth dynamics. We demonstrate that hematin crystals, crucial for the survival of malaria parasites, transition from faceted to rough growth interfaces at increasing thermodynamic supersaturation Δµ. Contrary to theoretical predictions and previous observations, this transition occurs at moderate values of Δµ. Moreover, surface roughness varies nonmonotonically with Δµ, and the rate constant for rough growth is slower than that resulting from nucleation and spreading of layers. We attribute these unexpected behaviors to the dynamics of step growth dominated by surface diffusion and the loss of identity of nuclei separated by less than the step width w. We put forth a general criterion for the onset of kinetic roughening using w as a critical length scale.
[Mh] Termos MeSH primário: Heme/química
Hemina/química
[Mh] Termos MeSH secundário: Cristalização
Difusão
Cinética
Modelos Químicos
Propriedades de Superfície
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
42VZT0U6YR (Heme); 743LRP9S7N (Hemin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevLett.119.198101


  2 / 3414 MEDLINE  
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[PMID]:29205135
[Au] Autor:Tada T; Uechi K; Nakasone I; Miyazato Z; Shinzato T; Shimada K; Tsuchiya M; Kirikae T; Fujita J
[Ad] Endereço:1​Department of Microbiology, Juntendo University School of Medicine, Tokyo, Japan.
[Ti] Título:A hemin auxotrophic Enterobacter cloacae clinical isolate with increased resistance to carbapenems and aminoglycosides.
[So] Source:J Med Microbiol;67(1):29-32, 2018 Jan.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Small-colony variants (SCVs) were obtained from an Enterobacter cloacae clinical isolate in Okinawa, Japan. One variant showed auxotrophy for hemin with a deletion of 20 365 nucleotides, dosC-ydiK-mmuP-mmuM-tauA-tauB-tauC-tauD-hemB-yaiT-yaiV-ampH-yddQ-sbmA-yaiW-yaiY-yaiZ, including hemB, and was more resistant to aminoglycosides and carbapenems, but more susceptible to aztreonam, than the parent strain.
[Mh] Termos MeSH primário: Aminoglicosídeos/farmacologia
Antibacterianos/farmacologia
Carbapenêmicos/farmacologia
Farmacorresistência Bacteriana Múltipla/efeitos dos fármacos
Enterobacter cloacae/efeitos dos fármacos
Enterobacter cloacae/isolamento & purificação
[Mh] Termos MeSH secundário: Aztreonam/farmacologia
Proteínas de Bactérias/genética
Enterobacter cloacae/genética
Hemina
Seres Humanos
Japão
Deleção de Sequência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Carbapenems); 743LRP9S7N (Hemin); G2B4VE5GH8 (Aztreonam)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000655


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[PMID]:28973477
[Au] Autor:Einarson OJ; Sen D
[Ad] Endereço:Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
[Ti] Título:Self-biotinylation of DNA G-quadruplexes via intrinsic peroxidase activity.
[So] Source:Nucleic Acids Res;45(17):9813-9822, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The striking and ubiquitous in vitro affinity between hemin and DNA/RNA G-quadruplexes raises the intriguing possibility of its relevance to biology. To date, no satisfactory experimental framework has been reported for investigating such a possibility. Complexation by G-quadruplexes leads to activation of the bound hemin toward catalysis of 1- and 2-electron oxidative reactions, with phenolic compounds being particularly outstanding substrates. We report here a strategy for exploiting that intrinsic peroxidase activity of hemin•G-quadruplex complexes for self-biotinylation of their G-quadruplex component. Such self-biotinylation occurs with good efficiency and high discrimination in vitro, being specific for G-quadruplexes and not for duplexes. The biotinylated DNA, moreover, remains amenable to polymerase chain reaction amplification, rendering it suitable for analysis by ChIP-Seq and related methods. We anticipate that this self-biotinylation methodology will also serve as a sensitive tool, orthogonal to existing ones, for identifying, labeling and pulling down cellular RNA and DNA G-quadruplexes in general, as well as proteins bound to or proximal to such quadruplexes.
[Mh] Termos MeSH primário: DNA Catalítico/química
Quadruplex G
Hemina/química
Oligonucleotídeos/química
Peroxidases/química
[Mh] Termos MeSH secundário: Biocatálise
Técnicas Biossensoriais/métodos
Biotina/química
Biotinilação
Peróxido de Hidrogênio/química
Cinética
Mimetismo Molecular
Oxirredução
Fenóis/química
Reação em Cadeia da Polimerase
Estreptavidina/química
Tiramina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Catalytic); 0 (Oligonucleotides); 0 (Phenols); 0 (biotin tyramine); 6SO6U10H04 (Biotin); 743LRP9S7N (Hemin); 9013-20-1 (Streptavidin); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); X8ZC7V0OX3 (Tyramine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx765


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[PMID]:28854095
[Au] Autor:Bissell DM; Anderson KE; Bonkovsky HL
[Ad] Endereço:From the Department of Medicine, Division of Gastroenterology and Porphyria Center, University of California, San Francisco, San Francisco (D.M.B.); the Departments of Preventive Medicine and Community Health and Internal Medicine, Division of Gastroenterology and Hepatology, University of Texas Medical Branch, Galveston (K.E.A.); and the Department of Gastroenterology, Wake Forest School of Medicine, Winston-Salem, NC (H.L.B.).
[Ti] Título:Porphyria.
[So] Source:N Engl J Med;377(9):862-872, 2017 Aug 31.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Porfiria Cutânea Tardia
Porfiria Aguda Intermitente
Protoporfiria Eritropoética
[Mh] Termos MeSH secundário: Feminino
Heme/biossíntese
Hemina/uso terapêutico
Seres Humanos
Masculino
Flebotomia
Porfobilinogênio/sangue
Porfiria Cutânea Tardia/complicações
Porfiria Cutânea Tardia/diagnóstico
Porfiria Cutânea Tardia/terapia
Porfiria Aguda Intermitente/complicações
Porfiria Aguda Intermitente/diagnóstico
Porfiria Aguda Intermitente/terapia
Porfirinas/análise
Prognóstico
Protoporfiria Eritropoética/complicações
Protoporfiria Eritropoética/diagnóstico
Protoporfiria Eritropoética/terapia
RNA Interferente Pequeno/uso terapêutico
Luz Solar/efeitos adversos
Avaliação de Sintomas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Porphyrins); 0 (RNA, Small Interfering); 42VZT0U6YR (Heme); 743LRP9S7N (Hemin); 74KHC72QXK (Porphobilinogen)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170831
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMra1608634


  5 / 3414 MEDLINE  
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[PMID]:28846391
[Au] Autor:Pires IS; Belcher DA; Palmer AF
[Ad] Endereço:William G. Lowrie Department of Chemical and Biomolecular Engineering, The Ohio State University , Columbus, Ohio 43210, United States.
[Ti] Título:Quantification of Active Apohemoglobin Heme-Binding Sites via Dicyanohemin Incorporation.
[So] Source:Biochemistry;56(40):5245-5259, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Apohemoglobin (apoHb) is produced by removing heme from hemoglobin (Hb). However, preparations of apoHb may contain damaged globins, which render total protein assays inaccurate for active apoHb quantification. Fortunately, apoHb heme-binding sites react with heme via the proximal histidine-F8 (His-F8) residue, which can be monitored spectrophotometrically. The bond between the His-F8 residue of apoHb and heme is vital for maintenance of fully functional and cooperative Hb. Additionally, most apoHb drug delivery applications facilitate hydrophobic drug incorporation inside the apoHb hydrophobic heme-binding pocket in which the His-F8 residue resides. This makes the His-F8 residue a proper target for apoHb activity quantification. In this work, dicyanohemin (DCNh), a stable monomeric porphyrin species, was used as a probe molecule to quantify active apoHb through monocyanohemin-His-F8 bond formation. ApoHb activity was quantified via the analysis of the 420 nm equilibrium absorbance of DCNh and apoHb mixtures. His-F8 saturation was determined by the presence of an inflection point from a plot of the 420 nm absorbance of a fixed concentration of apoHb against an increasing DCNh concentration. Various concentrations of a stock apoHb solution were tested to demonstrate the precision of the assay. The accuracy of the assay was assessed via spectral deconvolution, confirming His-F8 saturation at the inflection point. The effect of the heme-binding protein bovine serum albumin and precipitated apoHb on assay sensitivity was not significant. An analysis of the biophysical properties of reconstituted Hb confirmed heme-binding pocket activity. Taken together, this assay provides a simple and reliable method for determination of apoHb activity.
[Mh] Termos MeSH primário: Apoproteínas/química
Apoproteínas/metabolismo
Heme/metabolismo
Hemina/química
Hemina/metabolismo
Hemoglobinas/química
Hemoglobinas/metabolismo
Nitrilos/química
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Bovinos
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Soroalbumina Bovina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoproteins); 0 (Hemoglobins); 0 (Nitriles); 0 (apohemoglobin); 27432CM55Q (Serum Albumin, Bovine); 42VZT0U6YR (Heme); 743LRP9S7N (Hemin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00683


  6 / 3414 MEDLINE  
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[PMID]:28829595
[Au] Autor:Wu H; Yin J; Zhang J; Richards MP
[Ad] Endereço:National Center of Meat Quality, Safety Control, Jiangsu Innovation Center of Meat Production, Processing, College of Food Science, Technology, Nanjing Agricultural University , Nanjing 210095, P. R. China.
[Ti] Título:Factors Affecting Lipid Oxidation Due to Pig and Turkey Hemolysate.
[So] Source:J Agric Food Chem;65(36):8011-8017, 2017 Sep 13.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Turkey hemolysate promoted lipid oxidation in washed muscle more effectively than pig hemolysate, which was partly attributed to the greater ability of H O that formed during auto-oxidation to oxidize the avian hemoglobin (Hb). Turkey and pig hemolysate (2.5 µM Hb) exposed to 10 µM H O oxidized to 48% and 4% metHb, respectively. Catalase activity, which converts H O to water, was elevated in the pig hemolysate. The larger difference in Hb oxidation when comparing turkey and pig hemolysate in washed muscle (relative to their auto-oxidation rates) suggested that lipid oxidation products facilitated formation of metHb. Turkey metHb released hemin more readily than pig metHb, which coincided with turkey metHb promoting lipid oxidation more effectively than pig metHb. Ferryl Hb was not detected during storage of turkey or pig hemolysate in washed muscle, which suggested a minor role for hypervalent forms of Hb in the oxidation of the lipids.
[Mh] Termos MeSH primário: Lipídeos/química
Músculos/química
[Mh] Termos MeSH secundário: Animais
Hemina/química
Hemoglobinas/química
Hemólise
Peróxido de Hidrogênio/química
Carne/análise
Mioglobina/química
Oxirredução
Suínos
Perus
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Lipids); 0 (Myoglobin); 743LRP9S7N (Hemin); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02764


  7 / 3414 MEDLINE  
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[PMID]:28716864
[Au] Autor:Janciauskiene S; Tumpara S; Wiese M; Wrenger S; Vijayan V; Gueler F; Chen R; Madyaningrana K; Mahadeva R; Welte T; Immenschuh S; Chorostowska-Wynimko J
[Ad] Endereço:Department of Respiratory Medicine, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Deutsches Zentrum für Lungenforschung, Hannover Medical School, Hannover, Germany; janciauskiene.sabina@mh-hannover.de.
[Ti] Título:Alpha1-antitrypsin binds hemin and prevents oxidative activation of human neutrophils: putative pathophysiological significance.
[So] Source:J Leukoc Biol;102(4):1127-1141, 2017 Oct.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heme is a ubiquitous compound of human tissues, and it is involved in cellular physiology and metabolism. Once released from the cell, free heme oxidizes to the ferric state (hemin). High levels of hemin can cause oxidative stress and inflammation if not neutralized immediately by specialized scavenger proteins. Human alpha1-antitrypsin (A1AT), an acute-phase glycoprotein and important inhibitor of neutrophil proteases, is also a hemin-binding protein. A short-term exposure of freshly isolated human blood neutrophils to 4 µM hemin results in cell spreading, surface expression of filament protein, vimentin, free radical production, expression of heme oxygenase-1 (HO-1), release of IL-8, and enhanced neutrophil adhesion to human endothelial cells. Consequently, the phosphorylation of protein kinase C (PKC) occurs after 25 min. Under the same experimental conditions, addition of 1 mg/ml A1AT markedly reduces or abolishes neutrophil-activating effects of hemin and prevents PKC phosphorylation. In a mouse model of acute kidney injury (AKI) plus injection of hemin, monotherapy with 4 mg/mouse A1AT significantly lowered serum levels of free hemin at 2 h after surgery. Moreover, a tendency toward lower AKI scores, reduced infiltration of neutrophils, and lower levels of serum chemokine [CXCL1/keratinocyte-derived chemokine (KC)] was observed. Our findings highlight A1AT as a potential serum scavenger of hemin and suggest that the commercial preparations of human plasma A1AT might prove to be useful therapeutics in conditions associated with hemolysis.
[Mh] Termos MeSH primário: Hemina/metabolismo
Ativação de Neutrófilo
Neutrófilos/metabolismo
alfa 1-Antitripsina/metabolismo
[Mh] Termos MeSH secundário: Lesão Renal Aguda/metabolismo
Lesão Renal Aguda/patologia
Animais
Modelos Animais de Doenças
Heme Oxigenase-1/metabolismo
Hemólise
Seres Humanos
Interleucina-8/metabolismo
Camundongos
Neutrófilos/patologia
Oxirredução
Proteína Quinase C/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL8 protein, human); 0 (Interleukin-8); 0 (alpha 1-Antitrypsin); 743LRP9S7N (Hemin); EC 1.14.14.18 (HMOX1 protein, human); EC 1.14.14.18 (Heme Oxygenase-1); EC 2.7.11.13 (Protein Kinase C)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3A0317-124R


  8 / 3414 MEDLINE  
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[PMID]:28551230
[Au] Autor:Yin J; Zhang W; Richards MP
[Ad] Endereço:Meat Science and Muscle Biology Laboratory, Department of Animal Sciences, University of Wisconsin-Madison, Madison, WI 53706, USA.
[Ti] Título:Attributes of lipid oxidation due to bovine myoglobin, hemoglobin and hemolysate.
[So] Source:Food Chem;234:230-235, 2017 Nov 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bovine hemolysate was purified by size exclusion chromatography, and one high molecular weight protein was detected relative to the hemoglobin (Hb) fraction. Purified Hb promoted lipid oxidation in washed muscle slightly but significantly better than hemolysate, which may have been due to the absence of catalase and peroxiredoxin in the purified Hb. Purified Hb auto-oxidized to metHb more rapidly than Hb in the hemolysate (P<0.05). OxyHb promoted lipid oxidation in washed muscle more effectively compared to oxyMb (P<0.05). This was ascribed to hemin, released from metHb, promoting lipid oxidation more readily than oxidative forms of Mb that retain their protoporphyrin moiety. A 3:1 ratio of Mb:Hb promoted lipid oxidation similarly compared to adding a 1:1 ratio of Mb:Hb to washed muscle. Lipid oxidation products due to Hb-mediated lipid oxidation were elevated 60-fold at pH 6.3 compared to pH 6.7.
[Mh] Termos MeSH primário: Hemoglobinas/química
Lipídeos/química
Mioglobina/química
[Mh] Termos MeSH secundário: Animais
Bovinos
Hemina/química
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Lipids); 0 (Myoglobin); 743LRP9S7N (Hemin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


  9 / 3414 MEDLINE  
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[PMID]:28533132
[Au] Autor:Cheng M; Zhou J; Jia G; Ai X; Mergny JL; Li C
[Ad] Endereço:State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China; University of Chinese Academy of Sciences, No. 19A Yuquan Road, Beijing 100049, China. Electronic address: mpcheng@dicp.ac.cn.
[Ti] Título:Relations between the loop transposition of DNA G-quadruplex and the catalytic function of DNAzyme.
[So] Source:Biochim Biophys Acta;1861(8):1913-1920, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The structures of DNA G-quadruplexes are essential for their functions in vivo and in vitro. Our present study revealed that sequential order of the three G-quadruplex loops, that is, loop transposition, could be a critical factor to determinate the G-quadruplex conformation and consequently improved the catalytic function of G-quadruplex based DNAzyme. In the presence of 100mM K , loop transposition induced one of the G-quadruplex isomers which shared identical loops but differed in the sequential order of loops into a hybrid topology while the others into predominately parallel topologies. D NMR spectroscopy and mutation analysis suggested that the hydrogen bonding from loops residues with nucleotides in flanking sequences may be responsible for the stabilization of the different conformations. A well-known DNAzyme consisting of G-quadruplex and hemin (Ferriprotoporphyrin IX chloride) was chosen to test the catalytic function. We found that the loop transposition could enhance the reaction rate obviously by increasing the hemin binding affinity to G-quadruplex. These findings disclose the relations between the loop transposition, G-quadruplex conformation and catalytic function of DNAzyme.
[Mh] Termos MeSH primário: Biocatálise
DNA Catalítico/fisiologia
Quadruplex G
[Mh] Termos MeSH secundário: Hemina/metabolismo
Ligações de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Catalytic); 743LRP9S7N (Hemin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE


  10 / 3414 MEDLINE  
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[PMID]:28499167
[Au] Autor:Zhao Y; Chu X; Yang B
[Ad] Endereço:Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Molecular Science, Key Laboratory of Materials for Energy Conversion and Storage of Shanxi Province, Shanxi University, Taiyuan 030006, China.
[Ti] Título:Electrochemical behavior of hemin binding with human centrin 3.
[So] Source:Bioelectrochemistry;117:15-22, 2017 Oct.
[Is] ISSN:1878-562X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The electrochemical responses of human centrin 3 (HsCen3) binding with hemin were studied by cyclic voltammetry (CV) and differential pulse voltammetry (DPV) using glassy carbon electrodes (GCEs). In CV, the formal potential (E ) of hemin with the addition of HsCen3 shifted from -0.51 to -0.36V (versus saturated calomel electrode, SCE), indicating that a new species of hemin-HsCen3 had formed. Upon binding with HsCen3, the redox current of hemin in CV and DPV decreased significantly. Based on their titration curves, the association constant of HsCen3 with hemin was obtained with a logK of approximately 4, which was consistent with that obtained from spectroscopy. Combining UV-Vis, fluorescence emission, and electrochemical methods, His100 located on the α-helix between the two domains of HsCen3 was identified as the ligand binding residue of hemin. The protein binding-induced change in electrochemical signal was thus used to construct the diffusion coefficient (D=1.43×10 cm /s), the charge-transfer coefficient (α=0.49), and electron transfer standard rate constant (k =2.54×10 s ) in the presence or absence of HsCen3. The electrochemical investigation of hemin bound with HsCen3 may provide useful data for understanding the biological processes of calcium-binding protein.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/química
Proteínas de Ligação ao Cálcio/metabolismo
Hemina/química
Hemina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carbono/química
Eletroquímica
Eletrodos
Vidro/química
Seres Humanos
Modelos Moleculares
Estresse Oxidativo
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CETN3 protein, human); 0 (Calcium-Binding Proteins); 743LRP9S7N (Hemin); 7440-44-0 (Carbon)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde