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  1 / 16332 MEDLINE  
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[PMID]:29351332
[Au] Autor:Grebenko A; Dremov V; Barzilovich P; Bubis A; Sidoruk K; Voeikova T; Gagkaeva Z; Chernov T; Korostylev E; Gorshunov B; Motovilov K
[Ad] Endereço:Moscow Institute of Physics and Technology, Institute lane 9, Dolgoprudny, Russian Federation.
[Ti] Título:Impedance spectroscopy of single bacterial nanofilament reveals water-mediated charge transfer.
[So] Source:PLoS One;13(1):e0191289, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For decades respiratory chain and photosystems were the main firing field of the studies devoted to mechanisms of electron transfer in proteins. The concept of conjugated lateral electron and transverse proton transport during cellular respiration and photosynthesis, which was formulated in the beginning of 1960-s, has been confirmed by thousands of experiments. However, charge transfer in recently discovered bacterial nanofilaments produced by various electrogenic bacteria is regarded currently outside of electron and proton conjugation concept. Here we report the new study of charge transfer within nanofilaments produced by Shewanella oneidensis MR-1 conducted in atmosphere of different relative humidity (RH). We utilize impedance spectroscopy and DC (direct current) transport measurements to find out the peculiarities of conductivity and Raman spectroscopy to analyze the nanofilaments' composition. Data analysis demonstrates that apparent conductivity of nanofilaments has crucial sensitivity to humidity and contains several components including one with unusual behavior which we assign to electron transport. We demonstrate that in the case of Shewanella oneidensis MR-1 charge transfer within these objects is strongly mediated by water. Basing on current data analysis of conductivity we conclude that the studied filaments of Shewanella oneidensis MR-1 are capable of hybrid (conjugated) electron and ion conductivity.
[Mh] Termos MeSH primário: Shewanella/metabolismo
Água/metabolismo
[Mh] Termos MeSH secundário: Citocromos/química
Citocromos/metabolismo
Espectroscopia Dielétrica
Transporte de Elétrons
Heme/metabolismo
Umidade
Shewanella/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochromes); 059QF0KO0R (Water); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191289


  2 / 16332 MEDLINE  
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[PMID]:29311464
[Au] Autor:Sato S; Tsushima M; Nakamura K; Nakamura H
[Ad] Endereço:Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology.
[Ti] Título:[Development and Application of Catalytic Tyrosine Modification].
[So] Source:Yakugaku Zasshi;138(1):39-46, 2018.
[Is] ISSN:1347-5231
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:The chemical labeling of proteins with synthetic probes is a key technique used in chemical biology, protein-based therapy, and material science. Much of the chemical labeling of native proteins, however, depends on the labeling of lysine and cysteine residues. While those methods have significantly contributed to native protein labeling, alternative methods that can modify different amino acid residues are still required. Herein we report the development of a novel methodology of tyrosine labeling, inspired by the luminol chemiluminescence reaction. Tyrosine residues are often exposed on a protein's surface and are thus expected to be good targets for protein functionalization. In our studies so far, we have found that 1) hemin oxidatively activates luminol derivatives as a catalyst, 2) N-methyl luminol derivative specifically forms a covalent bond with a tyrosine residue among the 20 kinds of natural amino acid residues, and 3) the efficiency of tyrosine labeling with N-methyl luminol derivative is markedly improved by using horseradish peroxidase (HRP) as a catalyst. We were able to use molecular oxygen as an oxidant under HRP/NADH conditions. By using these methods, the functionalization of purified proteins was carried out. Because N-methyl luminol derivative is an excellent protein labeling reagent that responds to the activation of peroxidase, this new method is expected to open doors to such biological applications as the signal amplification of HRP-conjugated antibodies and the detection of protein association in combination with peroxidase-tag technology.
[Mh] Termos MeSH primário: Tirosina/química
[Mh] Termos MeSH secundário: Catálise
Heme/química
Hemeproteínas/química
Luminescência
Luminol/química
Peroxidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Hemeproteins); 42HK56048U (Tyrosine); 42VZT0U6YR (Heme); 5EXP385Q4F (Luminol); EC 1.11.1.7 (Peroxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1248/yakushi.17-00186-1


  3 / 16332 MEDLINE  
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[PMID]:29260810
[Au] Autor:Chang S; Mizuno M; Ishikawa H; Mizutani Y
[Ad] Endereço:Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan. mztn@chem.sci.osaka-u.ac.jp.
[Ti] Título:Tertiary dynamics of human adult hemoglobin fixed in R and T quaternary structures.
[So] Source:Phys Chem Chem Phys;20(5):3363-3372, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein dynamics of human adult hemoglobin and its mutants restricted in R and T quaternary states following ligand photolysis were studied by time-resolved resonance Raman spectroscopy. In the time-resolved spectra, we observed spectral changes of in-plane stretching modes of heme and the iron-histidine stretching mode of the Fe-His bond for all the hemoglobin samples. The ßD99N mutant, which adopts the R state in both the ligand-bound and the deoxy forms, showed similar temporal behaviors in time-resolved resonance Raman spectra as wild-type recombinant hemoglobin until 10 µs, consistent with the fact that the mutant undergoes only the tertiary structural changes in the R state. The ßN102T mutant, which adopts the T state in both the ligand-bound and the deoxy forms, showed much slower tertiary structural changes, suggesting that the EF helical motion is decelerated by the change of the intersubunit interactions. The present data indicate that the allosteric kinetic response between the interhelical hydrogen bonds of the EF helices and the intersubunit hydrogen bonds is bidirectional. The implications of these results for understanding the allosteric pathway of Hb are discussed in detail.
[Mh] Termos MeSH primário: Hemoglobinas/química
[Mh] Termos MeSH secundário: Adulto
Heme/química
Heme/metabolismo
Hemoglobinas/genética
Hemoglobinas/metabolismo
Histidina/química
Histidina/metabolismo
Seres Humanos
Ligações de Hidrogênio
Mutagênese Sítio-Dirigida
Estrutura Quaternária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Recombinant Proteins); 42VZT0U6YR (Heme); 4QD397987E (Histidine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06287g


  4 / 16332 MEDLINE  
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[PMID]:28458145
[Au] Autor:Bischin C; Mot A; Stefancu A; Leopold N; Hathazi D; Damian G; Silaghi-Dumitrescu R
[Ad] Endereço:Department of Chemistry, Babes-Bolyai University, 11 Arany Janos Street, Cluj-Napoca 400028, Romania.
[Ti] Título:Chlorite reactivity with myoglobin: Analogy with peroxide and nitrite chemistry?
[So] Source:J Inorg Biochem;172:122-128, 2017 Jul.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stopped-flow UV-vis data allow for the first time direct spectroscopic detection of a ferryl species during the reaction of met myoglobin (Mb) with chlorite, analogous to what is observed in the reaction with peroxides. Ferryl is also observed in the reaction of oxy Mb+chlorite. A pathway involving Fe-O-O-ClO is explored by analogy with the Fe-O-O-NO and Fe-O-O-NO previously proposed as intermediates in the reactions of oxy globins with nitric oxide and nitrite, respectively. However, Fe-O-O-ClO is not detectable in these stopped-flow experiments and is in fact, unlike its nitrogenous congeners, predicted by density functional theory (DFT) to be impossible for a heme complex. Deoxy Mb reacts with chlorite faster than met - suggesting that, unlike with hydrogen peroxide (with which deoxy Mb reacts slower than met), binding of chlorite to the heme is not a rate-determining step (hence, most likely, an outer-sphere electron transfer mechanism); to correlate this, a Fe-O-Cl-O adduct was not observed experimentally for the met or for the deoxy reactions - even though prior DFT calculations suggest it to be feasible and detectable.
[Mh] Termos MeSH primário: Cloretos/química
Mioglobina/química
Nitritos/química
Peróxidos/química
Teoria Quântica
[Mh] Termos MeSH secundário: Heme/química
Modelos Químicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chlorides); 0 (Myoglobin); 0 (Nitrites); 0 (Peroxides); 42VZT0U6YR (Heme); Z63H374SB6 (chlorite)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  5 / 16332 MEDLINE  
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[PMID]:29284023
[Au] Autor:Kosugi N; Araki T; Fujita J; Tanaka S; Fujiwara T
[Ad] Endereço:Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, Japan.
[Ti] Título:Growth phenotype analysis of heme synthetic enzymes in a halophilic archaeon, Haloferax volcanii.
[So] Source:PLoS One;12(12):e0189913, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Halophilic euryarchaea lack many of the genes necessary for the protoporphyrin-dependent heme biosynthesis pathway previously identified in animals and plants. Bioinformatic analysis suggested the presence of two heme biosynthetic processes, an Fe-coproporphyrinogen III (coproheme) decarboxylase (ChdC) pathway and an alternative heme biosynthesis (Ahb) pathway, in Haloferax volcanii. PitA is specific to the halophilic archaea and has a unique molecular structure in which the ChdC domain is joined to the antibiotics biosynthesis monooxygenase (ABM)-like domain by a histidine-rich linker sequence. The pitA gene deletion variant of H. volcanii showed a phenotype with a significant reduction of aerobic growth. Addition of a protoheme complemented the phenotype, supporting the assumption that PitA participates in the aerobic heme biosynthesis. Deletion of the ahbD gene caused a significant reduction of only anaerobic growth by denitrification or dimethylsulfoxide (DMSO) respiration, and the growth was also complemented by addition of a protoheme. The experimental results suggest that the two heme biosynthesis pathways are utilized selectively under aerobic and anaerobic conditions in H. volcanii. The molecular structure and physiological function of PitA are also discussed on the basis of the limited proteolysis and sequence analysis.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Haloferax volcanii/crescimento & desenvolvimento
Heme/metabolismo
[Mh] Termos MeSH secundário: Deleção de Genes
Regulação da Expressão Gênica em Archaea
Haloferax volcanii/enzimologia
Haloferax volcanii/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189913


  6 / 16332 MEDLINE  
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[PMID]:29199120
[Au] Autor:Jorge SE; Bringas M; Petruk AA; Arrar M; Marti MA; Skaf MS; Costa FF; Capece L; Sonati MF; Estrin D
[Ad] Endereço:Department of Clinical Pathology, School of Medical Sciences, University of Campinas (Unicamp), Campinas, SP, Brazil.
[Ti] Título:Understanding the molecular basis of the high oxygen affinity variant human hemoglobin Coimbra.
[So] Source:Arch Biochem Biophys;637:73-78, 2018 01 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human hemoglobin (Hb) Coimbra (ßAsp99Glu) is one of the seven ßAsp99 Hb variants described to date. All ßAsp99 substitutions result in increased affinity for O and decreased heme-heme cooperativity and their carriers are clinically characterized by erythrocytocis, caused by tissue hypoxia. Since ßAsp99 plays an important role in the allosteric α1ß2 interface and the mutation in Hb Coimbra only represents the insertion of a CH group in this interface, the present study of Hb Coimbra is important for a better understanding of the global impact of small modifications in this allosteric interface. We carried out functional, kinetic and dynamic characterization of this hemoglobin, focusing on the interpretation of these results in the context of a growth of the position 99 side chain length in the α1ß2 interface. Oxygen affinity was evaluated by measuring p50 values in distinct pHs (Bohr effect), and the heme-heme cooperativity was analyzed by determining the Hill coefficient (n), in addition to the effect of the allosteric effectors inositol hexaphosphate (IHP) and 2,3-bisphosphoglyceric acid (2,3-BPG). Computer simulations revealed a stabilization of the R state in the Coimbra variant with respect to the wild type, and consistently, the T-to-R quaternary transition was observed on the nanosecond time scale of classical molecular dynamics simulations.
[Mh] Termos MeSH primário: Hemoglobinas Anormais/química
Hemoglobinas Anormais/metabolismo
[Mh] Termos MeSH secundário: 2,3-Difosfoglicerato/farmacologia
Regulação Alostérica
Heme/metabolismo
Hemoglobinas Anormais/genética
Seres Humanos
Técnicas In Vitro
Cinética
Modelos Moleculares
Simulação de Dinâmica Molecular
Oxigênio/metabolismo
Ácido Fítico/farmacologia
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemoglobins, Abnormal); 138-81-8 (2,3-Diphosphoglycerate); 139735-68-5 (hemoglobin Coimbra); 42VZT0U6YR (Heme); 7IGF0S7R8I (Phytic Acid); S88TT14065 (Oxygen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  7 / 16332 MEDLINE  
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[PMID]:28739446
[Au] Autor:Panneerselvam S; Shehzad A; Mueller-Dieckmann J; Wilmanns M; Bocola M; Davari MD; Schwaneberg U
[Ad] Endereço:HASYLAB, DESY, Notkestrasse 85, 22603 Hamburg, Germany.
[Ti] Título:Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
[So] Source:Biochim Biophys Acta;1866(1):134-140, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source. The crystal structure shows a binding site for the mediator cobalt (III) sepulchrate at the entrance of the substrate access channel. The mediator occupies an unusual position which is far from the active site and distinct from the binding of the natural redox partner (FAD/NADPH binding domain).
[Mh] Termos MeSH primário: Bacillus megaterium/química
Proteínas de Bactérias/química
Cobalto/química
Coenzimas/química
Sistema Enzimático do Citocromo P-450/química
Elétrons
Heme/química
NADPH-Ferri-Hemoproteína Redutase/química
NADP/química
[Mh] Termos MeSH secundário: Bacillus megaterium/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cobalto/metabolismo
Coenzimas/metabolismo
Cristalografia por Raios X
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Heme/metabolismo
Modelos Moleculares
NADP/metabolismo
NADPH-Ferri-Hemoproteína Redutase/genética
NADPH-Ferri-Hemoproteína Redutase/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Zinco/química
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Recombinant Proteins); 3G0H8C9362 (Cobalt); 42VZT0U6YR (Heme); 53-59-8 (NADP); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase); EC 1.6.2.4 (flavocytochrome P450 BM3 monoxygenases); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  8 / 16332 MEDLINE  
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[PMID]:28668640
[Au] Autor:Mak PJ; Denisov IG
[Ad] Endereço:Department of Chemistry, Saint Louis University, St. Louis, MO, United States. Electronic address: makp@slu.edu.
[Ti] Título:Spectroscopic studies of the cytochrome P450 reaction mechanisms.
[So] Source:Biochim Biophys Acta;1866(1):178-204, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often under physiological conditions, catalyze many distinct oxidative transformations on a wide variety of molecules, including relatively simple alkanes or fatty acids, as well as more complex compounds such as steroids and exogenous pollutants. They perform such impressive chemistry utilizing a sophisticated catalytic cycle that involves a series of consecutive chemical transformations of heme prosthetic group. Each of these steps provides a unique spectral signature that reflects changes in oxidation or spin states, deformation of the porphyrin ring or alteration of dioxygen moieties. For a long time, the focus of cytochrome P450 research was to understand the underlying reaction mechanism of each enzymatic step, with the biggest challenge being identification and characterization of the powerful oxidizing intermediates. Spectroscopic methods, such as electronic absorption (UV-Vis), electron paramagnetic resonance (EPR), nuclear magnetic resonance (NMR), electron nuclear double resonance (ENDOR), Mössbauer, X-ray absorption (XAS), and resonance Raman (rR), have been useful tools in providing multifaceted and detailed mechanistic insights into the biophysics and biochemistry of these fascinating enzymes. The combination of spectroscopic techniques with novel approaches, such as cryoreduction and Nanodisc technology, allowed for generation, trapping and characterizing long sought transient intermediates, a task that has been difficult to achieve using other methods. Results obtained from the UV-Vis, rR and EPR spectroscopies are the main focus of this review, while the remaining spectroscopic techniques are briefly summarized. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/química
Heme/química
Ferro/química
Oxigênio/química
[Mh] Termos MeSH secundário: Biocatálise
Espectroscopia de Ressonância de Spin Eletrônica/instrumentação
Espectroscopia de Ressonância de Spin Eletrônica/métodos
Radicais Livres/química
Congelamento
Glicerol/química
Espectroscopia de Ressonância Magnética/instrumentação
Espectroscopia de Ressonância Magnética/métodos
Modelos Moleculares
Oxirredução
Estrutura Secundária de Proteína
Análise Espectral Raman/instrumentação
Análise Espectral Raman/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Free Radicals); 42VZT0U6YR (Heme); 9035-51-2 (Cytochrome P-450 Enzyme System); E1UOL152H7 (Iron); PDC6A3C0OX (Glycerol); S88TT14065 (Oxygen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


  9 / 16332 MEDLINE  
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[PMID]:28599858
[Au] Autor:Shalan H; Kato M; Cheruzel L
[Ad] Endereço:San José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
[Ti] Título:Keeping the spotlight on cytochrome P450.
[So] Source:Biochim Biophys Acta;1866(1):80-87, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This review describes the recent advances utilizing photosensitizers and visible light to harness the synthetic potential of P450 enzymes. The structures of the photosensitizers investigated to date are first presented along with their photophysical and redox properties. Functional photosensitizers range from organic and inorganic complexes to nanomaterials as well as the biological photosystem I complex. The focus is then on the three distinct approaches that have emerged for the activation of P450 enzymes. The first approach utilizes the in situ generation of reactive oxygen species entering the P450 mechanism via the peroxide shunt pathway. The other two approaches are sustained by electron injections into catalytically competent heme domains either facilitated by redox partners or through direct heme domain reduction. Achievements as well as pitfalls of each approach are briefly summarized. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/química
Elétrons
Escherichia coli/enzimologia
Heme/química
Complexos de Proteínas Captadores de Luz/química
Fármacos Fotossensibilizantes/química
[Mh] Termos MeSH secundário: Biocatálise
Compostos de Cádmio/química
Sistema Enzimático do Citocromo P-450/metabolismo
Amarelo de Eosina-(YS)/química
Amarelo de Eosina-(YS)/metabolismo
Escherichia coli/química
Escherichia coli/efeitos da radiação
Heme/metabolismo
Luz
Complexos de Proteínas Captadores de Luz/metabolismo
Modelos Moleculares
Oxirredução
Peróxidos/química
Peróxidos/metabolismo
Fármacos Fotossensibilizantes/metabolismo
Estrutura Secundária de Proteína
Pontos Quânticos
Sulfetos/química
Superóxidos/química
Superóxidos/metabolismo
Tioglicolatos/química
Tioglicolatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Cadmium Compounds); 0 (Light-Harvesting Protein Complexes); 0 (Peroxides); 0 (Photosensitizing Agents); 0 (Sulfides); 0 (Thioglycolates); 057EZR4Z7Q (cadmium sulfide); 11062-77-4 (Superoxides); 42VZT0U6YR (Heme); 7857H94KHM (2-mercaptoacetate); 9035-51-2 (Cytochrome P-450 Enzyme System); TDQ283MPCW (Eosine Yellowish-(YS))
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170611
[St] Status:MEDLINE


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[PMID]:28473297
[Au] Autor:Pochapsky TC; Wong N; Zhuang Y; Futcher J; Pandelia ME; Teitz DR; Colthart AM
[Ad] Endereço:Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454-9110, USA. Electronic address: pochapsk@brandeis.edu.
[Ti] Título:NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450.
[So] Source:Biochim Biophys Acta;1866(1):126-133, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The existence of a substrate-sensitive equilibrium between high spin (S=5/2) and low spin (S=1/2) ferric iron is a well-established phenomenon in the cytochrome P450 (CYP) superfamily, although its origins are still a subject of discussion. A series of mutations that strongly perturb the spin state equilibrium in the camphor hydroxylase CYP101A1 were recently described (Colthart et al., Sci. Rep. 6, 22035 (2016)). Wild type CYP101A1 as well as some CYP101A1 mutants are herein shown to be capable of catalyzing the reduction of nitroacetophenones by NADH to the corresponding anilino compounds (nitroreductase or NRase activity). The distinguishing characteristic between those mutants that catalyze the reduction and those that cannot appears to be the extent to which residual high spin form exists in the absence of the native substrate d-camphor, with those showing the largest spin state shifts upon camphor binding also exhibiting NRase activity. Optical and EPR spectroscopy was used to further examine these phenomena. These results suggest that reduction of nitroaromatics may provide a useful probe of residual high spin states in the CYP superfamily. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Acetofenonas/química
Proteínas de Bactérias/química
Cânfora 5-Mono-Oxigenase/química
Cânfora/química
Compostos Férricos/química
Heme/química
NAD/química
[Mh] Termos MeSH secundário: Acetofenonas/metabolismo
Motivos de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Biocatálise
Cânfora/metabolismo
Cânfora 5-Mono-Oxigenase/genética
Cânfora 5-Mono-Oxigenase/metabolismo
Clonagem Molecular
Espectroscopia de Ressonância de Spin Eletrônica
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Heme/metabolismo
Cinética
Modelos Moleculares
NAD/metabolismo
Oxirredução
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Acetophenones); 0 (Bacterial Proteins); 0 (Ferric Compounds); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); 100-19-6 (4-nitroacetophenone); 42VZT0U6YR (Heme); 76-22-2 (Camphor); EC 1.14.15.1 (Camphor 5-Monooxygenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE



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