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Pesquisa : D12.776.097.100 [Categoria DeCS]
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  1 / 908 MEDLINE  
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[PMID]:28691165
[Au] Autor:Yamaguchi T; Nihei Y; Sutherland DEK; Stillman MJ; Kohzuma T
[Ad] Endereço:Graduate School of Science and Engineering, Institute of Quantum Beam Science, Ibaraki University, Mito, Ibaraki, 310-8512, Japan.
[Ti] Título:Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.
[So] Source:Protein Sci;26(10):1921-1931, 2017 Oct.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Noncovalent, weak interactions in the second coordination sphere of the copper active site of Pseudoazurin (PAz) from Achromobacter cycloclastes were examined using a series of Met16X variants. In this study, the differences in protein stability due to the changes in the nature of the 16th amino acid (Met, Phe, Val, Ile) were investigated by electrospray ionization mass spectrometry (ESI-MS) and far-UV circular dichroism (CD) as a result of acid denaturation. The percentage of native states (folded holo forms) of Met16Phe variants was estimated to be 75% at pH 2.9 although the wild-type (WT), Met16Val and Met16Ile PAz, became completely unfolded. The high stability under acidic conditions is correlated with the result of the active site being stabilized by the aromatic substitution of the Met16 residue. The π-π interaction in the second coordination sphere makes a significant contribution to the stability of active site and the protein matrix.
[Mh] Termos MeSH primário: Azurina/química
Azurina/metabolismo
[Mh] Termos MeSH secundário: Azurina/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Dicroísmo Circular
Cobre/química
Cobre/metabolismo
Modelos Moleculares
Estabilidade Proteica
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (pseudoazurin); 12284-43-4 (Azurin); 789U1901C5 (Copper)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3226


  2 / 908 MEDLINE  
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[PMID]:28214520
[Au] Autor:Roger M; Sciara G; Biaso F; Lojou E; Wang X; Bauzan M; Giudici-Orticoni MT; Vila AJ; Ilbert M
[Ad] Endereço:Aix-Marseille Univ, CNRS, BIP UMR 7281, 31 chemin J. Aiguier, 13009 Marseille Cedex 20, France.
[Ti] Título:Impact of copper ligand mutations on a cupredoxin with a green copper center.
[So] Source:Biochim Biophys Acta;1858(5):351-359, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and a methionine. The recent discovery of new members of this family with unusual properties demonstrates, however, the versatility of this class of proteins. Changes in their ligand set lead to drastic variation in their metal site geometry and in the resulting spectroscopic and redox features. In our work, we report the identification of the copper ligands in the recently discovered cupredoxin AcoP. We show that even though AcoP possesses a classical copper ligand set, it has a highly perturbed copper center. In depth studies of mutant's properties suggest a high degree of constraint existing in the copper center of the wild type protein and even the addition of exogenous ligands does not lead to the reconstitution of the initial copper center. Not only the chemical nature of the axial ligand but also constraints brought by its covalent binding to the protein backbone might be critical to maintain a green copper site with high redox potential. This work illustrates the importance of experimentally dissecting the molecular diversity of cupredoxins to determine the molecular determinants responsible for their copper center geometry and redox potential.
[Mh] Termos MeSH primário: Acidithiobacillus/metabolismo
Azurina/metabolismo
Proteínas de Bactérias/metabolismo
Cobre/metabolismo
Mutação
[Mh] Termos MeSH secundário: Acidithiobacillus/genética
Azurina/química
Azurina/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Dicroísmo Circular
Cobre/química
Espectroscopia de Ressonância de Spin Eletrônica
Genótipo
Concentração de Íons de Hidrogênio
Ligantes
Oxirredução
Fenótipo
Ligação Proteica
Conformação Proteica
Espectrofotometria Ultravioleta
Relação Estrutura-Atividade
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Ligands); 0 (cupredoxin); 12284-43-4 (Azurin); 789U1901C5 (Copper)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170220
[St] Status:MEDLINE


  3 / 908 MEDLINE  
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[PMID]:27957837
[Au] Autor:Kleingardner EC; Asher WB; Bren KL
[Ad] Endereço:Department of Chemistry, University of Rochester , Rochester, New York 14627-0216, United States.
[Ti] Título:Efficient and Flexible Preparation of Biosynthetic Microperoxidases.
[So] Source:Biochemistry;56(1):143-148, 2017 Jan 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heme peptides and their derivatives, also called microperoxidases (MPs), are employed as heme protein active site models, catalysts, and charge-transfer chromophores. In this work, two approaches to the biosynthesis of novel MPs are described. In one method, heme peptides are expressed as C-terminal tags to the protein azurin and the MP is liberated by proteolytic cleavage by an endopeptidase. In an alternative approach, heme peptides are expressed as N-terminal tags to the cysteine protease domain (CPD) of the Vibrio cholerae MARTX toxin. Once activated by inositol hexakisphosphate, CPD undergoes autocleavage at an N-terminal leucine residue to liberate the MP. Purification is aided by use of a histidine-immobilized Sepharose column that binds exposed heme [Asher, W. A., and Bren, K. L. (2010) Protein Sci. 19, 1830-1839]. These methods provide efficient and adaptable routes to the preparation of a wide range of biosynthetic heme peptides.
[Mh] Termos MeSH primário: Heme/metabolismo
Peptídeos/metabolismo
Peroxidases/biossíntese
Proteínas Recombinantes/biossíntese
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Azurina/química
Azurina/genética
Azurina/metabolismo
Toxinas Bacterianas/química
Toxinas Bacterianas/genética
Toxinas Bacterianas/metabolismo
Dicroísmo Circular
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Heme/química
Heme/genética
Modelos Moleculares
Estrutura Molecular
Peptídeos/química
Peptídeos/genética
Peroxidases/química
Peroxidases/genética
Conformação Proteica
Proteínas Recombinantes/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Peptides); 0 (Recombinant Proteins); 0 (RtxA protein, Vibrio cholerae); 12284-43-4 (Azurin); 42VZT0U6YR (Heme); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (microperoxidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00915


  4 / 908 MEDLINE  
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[PMID]:27871046
[Au] Autor:Yagati AK; Kim SU; Lee T; Min J; Choi JW
[Ad] Endereço:Department of Biomedical Engineering, Sogang University, Seoul, 04107, Republic of Korea; Department of Biomedical Engineering, Gachon University, Incheon, 21936, Republic of Korea.
[Ti] Título:Recombinant azurin-CdSe/ZnS hybrid structures for nanoscale resistive random access memory device.
[So] Source:Biosens Bioelectron;90:23-30, 2017 Apr 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the present study, we developed a biohybrid material composed of recombinant azurin and CdSe-ZnS quantum dot to perform as a resistive random access memory (ReRAM) device. Site specific amino acid sequences were introduced in azurin to bind with the surface of CdSe-ZnS nanoparticle allowing the formation of a hybrid and voltage-driven switching enabled to develop a resistive random access memory (ReRAM) device. The analytical measurements confirmed that the azurin and CdSe-ZnS nanoparticles were well conjugated and formed into a single hybrid. Further, reversible, bistable switching along with repeatable writing-reading-erasing processes on individual azurin/CdSe-ZnS hybrid at nanoscale was achieved on the hybrid device. The device was programmed tested for 50 cycles with an ON/OFF ratio and measured to be of three orders of magnitude. The developed device shown good stability and repeatability and operates at low voltages thus makes it promising candidate for future memory device applications.
[Mh] Termos MeSH primário: Azurina/química
Técnicas Biossensoriais/instrumentação
Nanopartículas/química
Nanotecnologia/instrumentação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Azurina/genética
Técnicas Biossensoriais/métodos
Compostos de Cádmio/química
Nanotecnologia/métodos
Pontos Quânticos/química
Compostos de Selênio/química
Processamento de Sinais Assistido por Computador
Zinco/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadmium Compounds); 0 (Selenium Compounds); 12284-43-4 (Azurin); A7F646JC5C (cadmium selenide); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170223
[Lr] Data última revisão:
170223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161122
[St] Status:MEDLINE


  5 / 908 MEDLINE  
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[PMID]:27759897
[Au] Autor:Yu Y; Petrik ID; Chacón KN; Hosseinzadeh P; Chen H; Blackburn NJ; Lu Y
[Ad] Endereço:Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308, China.
[Ti] Título:Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.
[So] Source:Protein Sci;26(2):218-226, 2017 Feb.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type 1 copper (T1Cu) proteins are electron transfer (ET) proteins involved in many important biological processes. While the effects of changing primary and secondary coordination spheres in the T1Cu ET function have been extensively studied, few report has explored the effect of the overall protein structural perturbation on active site configuration or reduction potential of the protein, even though the protein scaffold has been proposed to play a critical role in enforcing the entatic or "rack-induced" state for ET functions. We herein report circular permutation of azurin by linking the N- and C-termini and creating new termini in the loops between 1 and 2 ß strands or between 3 and 4 ß strands. Characterization by electronic absorption, electron paramagnetic spectroscopies, as well as crystallography and cyclic voltammetry revealed that, while the overall structure and the primary coordination sphere of the circular permutated azurins remain the same as those of native azurin, their reduction potentials increased by 18 and 124 mV over that of WTAz. Such increases in reduction potentials can be attributed to subtle differences in the hydrogen-bonding network in secondary coordination sphere around the T1Cu center.
[Mh] Termos MeSH primário: Azurina/química
Cobre/química
[Mh] Termos MeSH secundário: Azurina/genética
Domínio Catalítico
Oxirredução
Estrutura Secundária de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
12284-43-4 (Azurin); 789U1901C5 (Copper)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3071


  6 / 908 MEDLINE  
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[PMID]:27918029
[Au] Autor:Clark KM; Tian S; van der Donk WA; Lu Y
[Ad] Endereço:Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue Urbana, IL 61801, USA. vddonk@illinois.edu yi-lu@illinois.edu.
[Ti] Título:Probing the role of the backbone carbonyl interaction with the Cu center in azurin by replacing the peptide bond with an ester linkage.
[So] Source:Chem Commun (Camb);53(1):224-227, 2016 12 20.
[Is] ISSN:1364-548X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The role of a backbone carbonyl interaction with an engineered Cu center in azurin was investigated by developing a method of synthesis and incorporation of a depsipeptide where one of the amide bonds in azurin is replaced by an ester bond using expressed protein ligation. Studies by electronic absorption and electron paramagnetic resonance spectroscopic techniques indicate that, while the substitution does not significantly alter the geometry of the site, it weakens the axial interaction to the Cu center and strengthens the Cu-Cu bond, as evidenced by the blue shift of the near-IR absorption that has been assigned to the Cu-Cu ψ → ψ* transition. Interestingly, the changes in the electronic structure from the replacement did not result in a change in the reduction potential of the Cu center, suggesting that the diamond core structure of Cu S is resistant to variations in axial interactions.
[Mh] Termos MeSH primário: Azurina/química
Azurina/metabolismo
Ésteres/química
Peptídeos/química
[Mh] Termos MeSH secundário: Azurina/genética
Modelos Moleculares
Conformação Proteica
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Esters); 0 (Peptides); 12284-43-4 (Azurin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161206
[St] Status:MEDLINE


  7 / 908 MEDLINE  
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[PMID]:27239476
[Au] Autor:Nguyen C; Nguyen VD
[Ad] Endereço:Theoretical Physics Research Group, Ton Duc Thang University, Ho Chi Minh City, Vietnam; Faculty of Applied Sciences, Ton Duc Thang University, Ho Chi Minh City, Vietnam.
[Ti] Título:Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53.
[So] Source:Biomed Res Int;2016:8490482, 2016.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Azurin from Pseudomonas aeruginosa is known anticancer bacteriocin, which can specifically penetrate human cancer cells and induce apoptosis. We hypothesized that pathogenic and commensal bacteria with long term residence in human body can produce azurin-like bacteriocins as a weapon against the invasion of cancers. In our previous work, putative bacteriocins have been screened from complete genomes of 66 dominant bacteria species in human gut microbiota and subsequently characterized by subjecting them as functional annotation algorithms with azurin as control. We have qualitatively predicted 14 putative bacteriocins that possessed functional properties very similar to those of azurin. In this work, we perform a number of quantitative and structure-based analyses including hydrophobic percentage calculation, structural modeling, and molecular docking study of bacteriocins of interest against protein p53, a cancer target. Finally, we have identified 8 putative bacteriocins that bind p53 in a same manner as p28-azurin and azurin, in which 3 peptides (p1seq16, p2seq20, and p3seq24) shared with our previous study and 5 novel ones (p1seq09, p2seq05, p2seq08, p3seq02, and p3seq17) discovered in the first time. These bacteriocins are suggested for further in vitro tests in different neoplastic line cells.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Azurina/farmacologia
Bacteriocinas/isolamento & purificação
Bacteriocinas/farmacologia
Microbioma Gastrointestinal/fisiologia
Trato Gastrointestinal/microbiologia
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos/isolamento & purificação
Estudos de Avaliação como Assunto
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Simulação de Acoplamento Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Bacteriocins); 0 (Tumor Suppressor Protein p53); 12284-43-4 (Azurin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160531
[St] Status:MEDLINE
[do] DOI:10.1155/2016/8490482


  8 / 908 MEDLINE  
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[PMID]:27096894
[Au] Autor:Bernardes N; Abreu S; Carvalho FA; Fernandes F; Santos NC; Fialho AM
[Ad] Endereço:a iBB-Institute for Bioengineering and Biosciences, Biological Sciences Research Group , Lisbon , Portugal.
[Ti] Título:Modulation of membrane properties of lung cancer cells by azurin enhances the sensitivity to EGFR-targeted therapy and decreased ß1 integrin-mediated adhesion.
[So] Source:Cell Cycle;15(11):1415-24, 2016 Jun 02.
[Is] ISSN:1551-4005
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In lung cancer, the Epidermal Growth Factor Receptor (EGFR) is one of the main targets for clinical management of this disease. The effectiveness of therapies toward this receptor has already been linked to the expression of integrin receptor subunit ß1 in NSCLC A549 cells. In this work we demonstrate that azurin, an anticancer therapeutic protein originated from bacterial cells, controls the levels of integrin ß1 and its appropriate membrane localization, impairing the intracellular signaling cascades downstream these receptors and the invasiveness of cells. We show evidences that azurin when combined with gefitinib and erlotinib, tyrosine kinase inhibitors which targets specifically the EGFR, enhances the sensitivity of these lung cancer cells to these molecules. The broad effect of azurin at the cell surface level was examined by Atomic Force Microscopy. The Young 's module (E) shows that the stiffness of A549 lung cancer cells decreased with exposure to azurin and also gefitinib, suggesting that the alterations in the membrane properties may be the basis of the broad anticancer activity of this protein. Overall, these results show that azurin may be relevant as an adjuvant to improve the effects of other anticancer agents already in clinical use, to which patients often develop resistance hampering its full therapeutic response.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Azurina/farmacologia
Membrana Celular/efeitos dos fármacos
Cloridrato de Erlotinib/farmacologia
Integrina beta1/genética
Quinazolinas/farmacologia
Receptor do Fator de Crescimento Epidérmico/genética
[Mh] Termos MeSH secundário: Células A549
Proteínas de Bactérias/farmacologia
Adesão Celular/efeitos dos fármacos
Membrana Celular/química
Membrana Celular/metabolismo
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Sinergismo Farmacológico
Módulo de Elasticidade
Matriz Extracelular/química
Matriz Extracelular/efeitos dos fármacos
Matriz Extracelular/metabolismo
Expressão Gênica
Seres Humanos
Integrina beta1/metabolismo
Microscopia de Força Atômica
Receptor do Fator de Crescimento Epidérmico/antagonistas & inibidores
Receptor do Fator de Crescimento Epidérmico/metabolismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Bacterial Proteins); 0 (Integrin beta1); 0 (Quinazolines); 12284-43-4 (Azurin); DA87705X9K (Erlotinib Hydrochloride); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); S65743JHBS (gefitinib)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160421
[St] Status:MEDLINE
[do] DOI:10.1080/15384101.2016.1172147


  9 / 908 MEDLINE  
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[PMID]:27055058
[Au] Autor:Berry SM; Strange JN; Bladholm EL; Khatiwada B; Hedstrom CG; Sauer AM
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Minnesota Duluth , 1039 University Drive, Duluth, Minnesota 55812, United States.
[Ti] Título:Nitrite Reductase Activity in Engineered Azurin Variants.
[So] Source:Inorg Chem;55(9):4233-47, 2016 05 02.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitrite reductase (NiR) activity was examined in a series of dicopper P.a. azurin variants in which a surface binding copper site was added through site-directed mutagenesis. Four variants were synthesized with copper binding motifs inspired by the catalytic type 2 copper binding sites found in the native noncoupled dinuclear copper enzymes nitrite reductase and peptidylglycine α-hydroxylating monooxygenase. The four azurin variants, denoted Az-NiR, Az-NiR3His, Az-PHM, and Az-PHM3His, maintained the azurin electron transfer copper center, with the second designed copper site located over 13 Å away and consisting of mutations Asn10His,Gln14Asp,Asn16His-azurin, Asn10His,Gln14His,Asn16His-azurin, Gln8Met,Gln14His,Asn16His-azurin, and Gln8His,Gln14His,Asn16His-azurin, respectively. UV-visible absorption spectroscopy, EPR spectroscopy, and electrochemistry of the sites demonstrate copper binding as well as interaction with small exogenous ligands. The nitrite reduction activity of the variants was determined, including the catalytic Michaelis-Menten parameters. The variants showed activity (0.34-0.59 min(-1)) that was slower than that of native NiRs but comparable to that of other model systems. There were small variations in activity of the four variants that correlated with the number of histidines in the added copper site. Catalysis was found to be reversible, with nitrite produced from NO. Reactions starting with reduced azurin variants demonstrated that electrons from both copper centers were used to reduce nitrite, although steady-state catalysis required the T2 copper center and did not require the T1 center. Finally, experiments separating rates of enzyme reduction from rates of reoxidation by nitrite demonstrated that the reaction with nitrite was rate limiting during catalysis.
[Mh] Termos MeSH primário: Azurina/química
Nitrito Redutases/química
[Mh] Termos MeSH secundário: Ácido Ascórbico/química
Azurina/genética
Sítios de Ligação
Catálise
Cobre/química
Técnicas Eletroquímicas
Cinética
Mutagênese Sítio-Dirigida
Oxirredução
Engenharia de Proteínas
Nitrito de Sódio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
12284-43-4 (Azurin); 789U1901C5 (Copper); EC 1.7.- (Nitrite Reductases); M0KG633D4F (Sodium Nitrite); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160408
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.5b03006


  10 / 908 MEDLINE  
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[PMID]:27029516
[Au] Autor:Abdullin D; Hagelueken G; Schiemann O
[Ad] Endereço:Institute of Physical and Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53115 Bonn, Germany. schiemann@pc.uni-bonn.de.
[Ti] Título:Determination of nitroxide spin label conformations via PELDOR and X-ray crystallography.
[So] Source:Phys Chem Chem Phys;18(15):10428-37, 2016 Apr 21.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pulsed electron-electron double resonance (PELDOR or DEER) in combination with site-directed spin labelling has emerged as an important method for measuring nanometer distance constraints that are used to obtain coarse-grained structures of biomolecules or to follow their conformational changes. Translating measured spin-spin distances between spin labels into structural information requires taking the conformational flexibility of spin label side chains into account. Here, we present an analysis of orientation selective PELDOR data recorded on six singly MTSSL-labelled azurin mutants. The analysis yielded conformational MTSSL ensembles, which are considerably narrower than those predicted using in silico spin labeling methods but match well with spin label conformations found in the corresponding crystal structures. The possible reasons and consequences for predicting spin label conformers in the fold of biomolecules are discussed.
[Mh] Termos MeSH primário: Óxidos de Nitrogênio/química
Marcadores de Spin
[Mh] Termos MeSH secundário: Azurina/química
Cristalografia por Raios X
Espectroscopia de Ressonância de Spin Eletrônica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nitrogen Oxides); 0 (Spin Labels); 12284-43-4 (Azurin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1039/c6cp01307d



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