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  1 / 1342 MEDLINE  
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[PMID]:29048424
[Au] Autor:Batllori M; Molero-Luis M; Ormazabal A; Casado M; Sierra C; García-Cazorla A; Kurian M; Pope S; Heales SJ; Artuch R
[Ad] Endereço:Department of Clinical Biochemistry, Institut de Recerca Sant Joan de Déu (IRSJD), Barcelona, Spain.
[Ti] Título:Analysis of human cerebrospinal fluid monoamines and their cofactors by HPLC.
[So] Source:Nat Protoc;12(11):2359-2375, 2017 Nov.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The presence of monoamines and their cofactors (the pterins and vitamin B (pyridoxal phosphate (PLP))) in human cerebrospinal fluid (CSF) can be used as indicators of the biosynthesis and turnover of dopamine and serotonin in the brain. In addition, abnormalities in the CSF levels of these molecules are associated with various neurological diseases, including genetic diseases leading to dopamine and serotonin deficiency. Here, we provide a set of quantitative high-performance liquid-chromatography (HPLC) approaches to determine CSF levels of monoamines and their cofactors. This protocol describes step-by-step procedures for CSF sample preparation for the analysis of different molecules, HPLC calibration and analysis, and data quantification and interpretation. Unlike plasma/tissue/blood samples, CSF requires minimal sample preparation: in this protocol, only the analysis of PLP requires mixing with trichloroacetic acid to release the protein-bound vitamin, centrifugation, and mixing of the supernatant with phosphate buffer and sodium cyanide for derivatization in alkaline conditions. Monoamines are analyzed by HPLC with coulometric electrochemical detection (ED), pterins are analyzed by HPLC with coupled coulometric electrochemical and fluorescence detection, and PLP is analyzed by HPLC with fluorescence detection. The quantification of all compounds is achieved by external calibration procedures, and internal quality control and standards are analyzed in each run. We anticipate that investigation of dopamine and serotonin disturbances will be facilitated by measurements of these compounds in human CSF and other biological samples. The estimated time for the different procedures primarily depends on the electrochemical detector stabilization. Overnight stabilization of this detector is advised, and, after that step, preanalytical equilibration rarely exceeds 3 h.
[Mh] Termos MeSH primário: Monoaminas Biogênicas/líquido cefalorraquidiano
Cromatografia Líquida de Alta Pressão/métodos
Pterinas/líquido cefalorraquidiano
Vitamina B 6/líquido cefalorraquidiano
[Mh] Termos MeSH secundário: Calibragem
Seres Humanos
Controle de Qualidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biogenic Monoamines); 0 (Pterins); 8059-24-3 (Vitamin B 6)
[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:171020
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.103


  2 / 1342 MEDLINE  
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[PMID]:28284029
[Au] Autor:Leimkühler S
[Ad] Endereço:.
[Ti] Título:Shared function and moonlighting proteins in molybdenum cofactor biosynthesis.
[So] Source:Biol Chem;398(9):1009-1026, 2017 Aug 28.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The biosynthesis of the molybdenum cofactor (Moco) is a highly conserved pathway in bacteria, archaea and eukaryotes. The molybdenum atom in Moco-containing enzymes is coordinated to the dithiolene group of a tricyclic pyranopterin monophosphate cofactor. The biosynthesis of Moco can be divided into three conserved steps, with a fourth present only in bacteria and archaea: (1) formation of cyclic pyranopterin monophosphate, (2) formation of molybdopterin (MPT), (3) insertion of molybdenum into MPT to form Mo-MPT, and (4) additional modification of Mo-MPT in bacteria with the attachment of a GMP or CMP nucleotide, forming the dinucleotide variants of Moco. While the proteins involved in the catalytic reaction of each step of Moco biosynthesis are highly conserved among the Phyla, a surprising link to other cellular pathways has been identified by recent discoveries. In particular, the pathways for FeS cluster assembly and thio-modifications of tRNA are connected to Moco biosynthesis by sharing the same protein components. Further, proteins involved in Moco biosynthesis are not only shared with other pathways, but additionally have moonlighting roles. This review gives an overview of Moco biosynthesis in bacteria and humans and highlights the shared function and moonlighting roles of the participating proteins.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Proteínas de Bactérias/metabolismo
Coenzimas/biossíntese
Metaloproteínas/biossíntese
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Compostos Organofosforados/metabolismo
Pteridinas
Pterinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Bacterial Proteins); 0 (Coenzymes); 0 (Metalloproteins); 0 (Organophosphorus Compounds); 0 (Pteridines); 0 (Pterins); 4X7K2681Y7 (cyclic pyranopterin monophosphate); 73508-07-3 (molybdenum cofactor)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE


  3 / 1342 MEDLINE  
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[PMID]:27815627
[Au] Autor:Ragone F; Saavedra HH; García PF; Wolcan E; Argüello GA; Ruiz GT
[Ad] Endereço:INIFTA, UNLP, (CCT La Plata-CONICET), Diag. 113 y 64, C.C. 16, Suc. 4, B1906ZAA, La Plata, Argentina.
[Ti] Título:Association studies to transporting proteins of fac-Re (CO) (pterin)(H O) complex.
[So] Source:J Biol Inorg Chem;22(1):99-108, 2017 Jan.
[Is] ISSN:1432-1327
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A new synthetic route to acquire the water soluble complex fac-Re (CO) (pterin)(H O) was carried out in aqueous solution. The complex has been obtained with success via the fac-[Re (CO) (H O) ]Cl precursor complex. Re (CO) (pterin)(H O) has been found to bind strongly with bovine and human serum albumins (BSA and HSA) with intrinsic-binding constants, K , of 6.5 × 10 M and 5.6 × 10 M at 310 K, respectively. The interactions of serum albumins with Re (CO) (pterin)(H O) were evaluated employing UV-vis fluorescence and absorption spectroscopy and circular dichroism. The results suggest that the serum albumins-Re (CO) (pterin)(H O) interactions occurred in the domain IIA-binding pocket without loss of helical stability of the proteins. The comparison of the fluorescence quenching of BSA and HSA due to the binding to the Re(I) complex suggested that local interaction around the Trp 214 residue had taken place. The analysis of the thermodynamic parameters ΔG , ΔH , and ΔS indicated that the hydrophobic interactions played a major role in both HSA-Re(I) and BSA-Re(I) association processes. All these experimental results suggest that these proteins can be considered as good carriers for transportation of Re (CO) (pterin)(H O) complex. This is of significant importance in relation to the use of this Re(I) complex in several biomedical fields, such as photodynamic therapy and radiopharmacy.
[Mh] Termos MeSH primário: Compostos Organometálicos/química
Compostos Organometálicos/metabolismo
Pterinas/química
Rênio/química
Soroalbumina Bovina/metabolismo
Água/química
[Mh] Termos MeSH secundário: Animais
Bovinos
Seres Humanos
Modelos Moleculares
Conformação Proteica em alfa-Hélice
Estabilidade Proteica
Solubilidade
Análise Espectral
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organometallic Compounds); 0 (Pterins); 059QF0KO0R (Water); 27432CM55Q (Serum Albumin, Bovine); 7440-15-5 (Rhenium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE
[do] DOI:10.1007/s00775-016-1410-7


  4 / 1342 MEDLINE  
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[PMID]:27580420
[Au] Autor:Lemaire ON; Bouillet S; Méjean V; Iobbi-Nivol C; Genest O
[Ad] Endereço:a Aix Marseille Univ, CNRS, BIP , Marseille , France.
[Ti] Título:Chaperones in maturation of molybdoenzymes: Why specific is better than general?
[So] Source:Bioengineered;8(2):133-136, 2017 Mar 04.
[Is] ISSN:2165-5987
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Molybdoenzymes play essential functions in living organisms and, as a result, in various geochemical cycles. It is thus crucial to understand how these complex proteins become highly efficient enzymes able to perform a wide range of catalytic activities. It has been established that specific chaperones are involved during their maturation process. Here, we raise the question of the involvement of general chaperones acting in concert with dedicated chaperones or not.
[Mh] Termos MeSH primário: Coenzimas/química
Coenzimas/metabolismo
Metaloproteínas/química
Metaloproteínas/metabolismo
Chaperonas Moleculares/química
Chaperonas Moleculares/metabolismo
Pteridinas/química
Pteridinas/metabolismo
[Mh] Termos MeSH secundário: Apoenzimas/química
Apoenzimas/metabolismo
Modelos Biológicos
Pterinas/química
Pterinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Coenzymes); 0 (Metalloproteins); 0 (Molecular Chaperones); 0 (Pteridines); 0 (Pterins); 0 (pyranopterin); 73508-07-3 (molybdenum cofactor)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160901
[St] Status:MEDLINE
[do] DOI:10.1080/21655979.2016.1218579


  5 / 1342 MEDLINE  
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[PMID]:27951655
[Au] Autor:Gao K; Jia Y; Yang M
[Ad] Endereço:Institute of Biophysics and Department of Physics, Central China Normal University , Wuhan 430079, P. R. China.
[Ti] Título:A Network of Conformational Transitions Revealed by Molecular Dynamics Simulations of the Binary Complex of Escherichia coli 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase with MgATP.
[So] Source:Biochemistry;55(49):6931-6939, 2016 Dec 13.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the first reaction in the folate biosynthetic pathway. Comparison of its X-ray and nuclear magnetic resonance structures suggests that the enzyme undergoes significant conformational change upon binding to its substrates, especially in three catalytic loops. Experimental research has shown that, in its binary form, even bound by analogues of MgATP, loops 2 and 3 remain rather flexible; this raises questions about the putative large-scale induced-fit conformational change of the HPPK-MgATP binary complex. In this work, long-time all-atomic molecular dynamics simulations were conducted to investigate the loop dynamics in this complex. Our simulations show that, with loop 3 closed, multiple conformations of loop 2, including the open, semiopen, and closed forms, are all accessible to the binary complex. These results provide valuable structural insights into the details of conformational changes upon 6-hydroxymethyl-7,8-dihydropterin (HP) binding and biological activities of HPPK. Conformational network analysis and principal component analysis related to the loops are also discussed.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Difosfotransferases/metabolismo
Escherichia coli/enzimologia
Simulação de Dinâmica Molecular
Pterinas/metabolismo
[Mh] Termos MeSH secundário: Ligações de Hidrogênio
Conformação Molecular
Análise de Componente Principal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-hydroxymethyl-7,8-dihydropterin); 0 (Pterins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.6.- (Diphosphotransferases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE


  6 / 1342 MEDLINE  
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[PMID]:27798097
[Au] Autor:Ishikawa T; Imamura K; Kondo T; Koshiba Y; Hara S; Ichinose H; Furujo M; Kinoshita M; Oeda T; Takahashi J; Takahashi R; Inoue H
[Ad] Endereço:Center for iPS Cell Research and Application (CiRA), Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto, Japan.
[Ti] Título:Genetic and pharmacological correction of aberrant dopamine synthesis using patient iPSCs with BH4 metabolism disorders.
[So] Source:Hum Mol Genet;25(23):5188-5197, 2016 Dec 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dopamine (DA) is a neurotransmitter in the brain, playing a central role in several disease conditions, including tetrahydrobiopterin (BH4) metabolism disorders and Parkinson's disease (PD). BH4 metabolism disorders present a variety of clinical manifestations including motor disturbance via altered DA metabolism, since BH4 is a cofactor for tyrosine hydroxylase (TH), a rate-limiting enzyme for DA synthesis. Genetically, BH4 metabolism disorders are, in an autosomal recessive pattern, caused by a variant in genes encoding enzymes for BH4 synthesis or recycling, including 6-pyruvoyltetrahydropterin synthase (PTPS) or dihydropteridine reductase (DHPR), respectively. Although BH4 metabolism disorders and its metabolisms have been studied, it is unclear how gene variants cause aberrant DA synthesis in patient neurons. Here, we generated induced pluripotent stem cells (iPSCs) from BH4 metabolism disorder patients with PTPS or DHPR variants, corrected the gene variant in the iPSCs using the CRISPR/Cas9 system, and differentiated the BH4 metabolism disorder patient- and isogenic control iPSCs into midbrain DA neurons. We found that by the gene correction, the BH4 amount, TH protein level and extracellular DA level were restored in DA neuronal culture using PTPS deficiency iPSCs. Furthermore, the pharmacological correction by BH4 precursor sepiapterin treatment also improved the phenotypes of PTPS deficiency. These results suggest that patient iPSCs with BH4 metabolism disorders provide an opportunity for screening substances for treating aberrant DA synthesis-related disorders.
[Mh] Termos MeSH primário: Biopterina/análogos & derivados
Dopamina/genética
Células-Tronco Pluripotentes Induzidas/metabolismo
Doenças Metabólicas/genética
Doença de Parkinson/genética
[Mh] Termos MeSH secundário: Biopterina/metabolismo
Diferenciação Celular/genética
Dopamina/biossíntese
Neurônios Dopaminérgicos/metabolismo
Neurônios Dopaminérgicos/patologia
Genótipo
Seres Humanos
Cariótipo
Doenças Metabólicas/metabolismo
Doenças Metabólicas/patologia
Doença de Parkinson/metabolismo
Doença de Parkinson/patologia
Pterinas/metabolismo
Tirosina 3-Mono-Oxigenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pterins); 22150-76-1 (Biopterin); EC 1.14.16.2 (Tyrosine 3-Monooxygenase); EGX657432I (sapropterin); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddw339


  7 / 1342 MEDLINE  
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[PMID]:27666634
[Au] Autor:Saito R; Suzuki S; Sasaki K
[Ad] Endereço:Department of Chemistry, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan; Research Center for Materials with Integrated Properties, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
[Ti] Título:Pterin-7-carboxamides as a new class of aldose reductase inhibitors.
[So] Source:Bioorg Med Chem Lett;26(20):4870-4874, 2016 10 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aldose reductase is related to the onset and progression of diabetic complications, such as neuropathy, retinopathy, angiopathy, and so on: therefore molecules that are capable of inhibiting the enzyme are potential drugs for treatment of diabetic complications. Epalrestat is the sole aldose reductase inhibitor that is clinically used, but still has some drawbacks. Thus, the development of new aldose reductase inhibitors is still desired. We have synthesized a series of new pterin-7-carboxamides, and evaluated their in vitro inhibitory activities against human aldose reductase. All newly synthesized compounds exhibited the inhibitory activity. Among them, 1a having a glycine side chain exhibits the highest activity comparable to that of sorbinil, a highly active aldose reductase inhibitor. Molecular docking of 1a on the active site of the enzyme indicated this compound interacts with amino acid residues that are specific to the enzyme and related to suppressing side effects. Based on these results, we proved perin-7-carboxamides to be a new class of aldose reductase inhibitors, and particularly compound 1a was found to be a good candidate for further biological investigations as a drug for treatment of diabetic complications with fewer side effects.
[Mh] Termos MeSH primário: Aldeído Redutase/antagonistas & inibidores
Amidas/química
Inibidores Enzimáticos/farmacologia
Pterinas/farmacologia
[Mh] Termos MeSH secundário: Inibidores Enzimáticos/química
Pterinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amides); 0 (Enzyme Inhibitors); 0 (Pterins); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160927
[St] Status:MEDLINE


  8 / 1342 MEDLINE  
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[PMID]:27537049
[Au] Autor:Wang CH; Zhang C; Xing XH
[Ad] Endereço:a Key Laboratory for Industrial Biocatalysis, Ministry of Education of China, Institute of Biochemical Engineering , Department of Chemical Engineering , Tsinghua University , Beijing , People's Republic of China.
[Ti] Título:Xanthine dehydrogenase: An old enzyme with new knowledge and prospects.
[So] Source:Bioengineered;7(6):395-405, 2016 Nov.
[Is] ISSN:2165-5987
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Xanthine dehydrogenase (EC 1.17.1.4, XDH) is a typical and complex molybdenum-containing flavoprotein which has been extensively studied for over 110 years. This enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD or NADP as electron acceptor, and sometimes can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor. XDHs are widely distributed in all eukarya, bacteria and archaea domains, and are proposed to play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. The recent applications of XDHs include clinical detections of xanthine and hypoxanthine content in body fluidics, and other diagnostic biomarkers like inorganic phosphorus, 5'-nucleotidase and adenosine deaminase. XDHs can also find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin. In this commentary, we would outline the latest knowledge on occurrence, structure, biosynthesis, and recent advances of production and applications of XDH, and highlighted the need to develop XDHs with improved performances by gene prospecting and protein engineering, and protocols for efficient production of active XDHs in response to the increasing demands.
[Mh] Termos MeSH primário: Xantina Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: 5'-Nucleotidase/metabolismo
Adenosina Desaminase/metabolismo
Aldeídos/metabolismo
Animais
Biodegradação Ambiental
Seres Humanos
Óxido Nítrico/metabolismo
Oxirredução
Fósforo/metabolismo
Pterinas/metabolismo
Purinas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Ribavirina/metabolismo
Xantina Desidrogenase/genética
Xantina Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aldehydes); 0 (Pterins); 0 (Purines); 0 (Reactive Oxygen Species); 27YLU75U4W (Phosphorus); 31C4KY9ESH (Nitric Oxide); 49717AWG6K (Ribavirin); EC 1.17.1.4 (Xanthine Dehydrogenase); EC 1.17.3.2 (Xanthine Oxidase); EC 3.1.3.5 (5'-Nucleotidase); EC 3.5.4.4 (Adenosine Deaminase); W60KTZ3IZY (purine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160819
[St] Status:MEDLINE
[do] DOI:10.1080/21655979.2016.1206168


  9 / 1342 MEDLINE  
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[PMID]:27500308
[Au] Autor:Reid LO; Roman EA; Thomas AH; Dántola ML
[Ad] Endereço:Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (INIFTA), Departamento de Química, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, CCT La Plata-CONICET , Casilla de Correo 16, Sucursal 4, 1900 La Plata, Argentina.
[Ti] Título:Photooxidation of Tryptophan and Tyrosine Residues in Human Serum Albumin Sensitized by Pterin: A Model for Globular Protein Photodamage in Skin.
[So] Source:Biochemistry;55(34):4777-86, 2016 Aug 30.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human serum albumin (HSA) is the most abundant protein in the circulatory system. Oxidized albumin was identified in the skin of patients suffering from vitiligo, a depigmentation disorder in which the protection against ultraviolet (UV) radiation fails because of the lack of melanin. Oxidized pterins, efficient photosensitizers under UV-A irradiation, accumulate in the skin affected by vitiligo. In this work, we have investigated the ability of pterin (Ptr), the parent compound of oxidized pterins, to induce structural and chemical changes in HSA under UV-A irradiation. Our results showed that Ptr is able to photoinduce oxidation of the protein in at least two amino acid residues: tryptophan (Trp) and tyrosine (Tyr). HSA undergoes oligomerization, yielding protein structures whose molecular weight increases with irradiation time. The protein cross-linking, due to the formation of dimers of Tyr, does not significantly affect the secondary and tertiary structures of HSA. Trp is consumed in the photosensitized process, and N-formylkynurenine was identified as one of its oxidation products. The photosensitization of HSA takes place via a purely dynamic process, which involves the triplet excited state of Ptr. The results presented in this work suggest that protein photodamage mediated by endogenous photosensitizers can significantly contribute to the harmful effects of UV-A radiation on the human skin.
[Mh] Termos MeSH primário: Albumina Sérica/química
Albumina Sérica/efeitos da radiação
[Mh] Termos MeSH secundário: Reagentes para Ligações Cruzadas
Seres Humanos
Modelos Químicos
Oxirredução
Processos Fotoquímicos
Fármacos Fotossensibilizantes/química
Fármacos Fotossensibilizantes/efeitos da radiação
Pterinas/química
Pterinas/efeitos da radiação
Albumina Sérica/metabolismo
Pele/metabolismo
Pele/efeitos da radiação
Envelhecimento da Pele/efeitos da radiação
Triptofano/química
Triptofano/efeitos da radiação
Tirosina/química
Tirosina/efeitos da radiação
Raios Ultravioleta/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Photosensitizing Agents); 0 (Pterins); 0 (Serum Albumin); 42HK56048U (Tyrosine); 8DUH1N11BX (Tryptophan)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160809
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00420


  10 / 1342 MEDLINE  
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[PMID]:27432259
[Au] Autor:Young CG
[Ad] Endereço:Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria 3086, Australia. Electronic address: Charles.Young@latrobe.edu.au.
[Ti] Título:Chemical systems modeling the d Mo(V) states of molybdenum enzymes.
[So] Source:J Inorg Biochem;162:238-252, 2016 Sep.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This review focuses on the synthesis, properties and electron paramagnetic resonance (EPR), electron spin echo envelope modulation (ESEEM) and electron-nuclear double resonance (ENDOR) spectroscopy of mononuclear d oxo- and sulfido-Mo(V) complexes relevant to the understanding of the EPR-active Mo(V) forms of pterin-containing molybdenum enzymes.
[Mh] Termos MeSH primário: Elétrons
Proteínas com Ferro-Enxofre/química
Molibdênio/química
Oxirredutases/química
Pterinas/química
Sulfito Oxidase/química
Xantina Oxidase/química
[Mh] Termos MeSH secundário: Materiais Biomiméticos
Domínio Catalítico
Espectroscopia de Ressonância de Spin Eletrônica
Modelos Químicos
Modelos Moleculares
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Pterins); 81AH48963U (Molybdenum); EC 1.- (Oxidoreductases); EC 1.17.3.2 (Xanthine Oxidase); EC 1.8.3.1 (Sulfite Oxidase); EC 1.8.99.- (dimethyl sulfoxide reductase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160720
[St] Status:MEDLINE



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