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  1 / 25 MEDLINE  
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[PMID]:28638868
[Au] Autor:Martínez-Pérez EF; Hernández-Terán F; Serrano-Gallardo LB
[Ad] Endereço:Centro de Investigación Biomédicas (CIBM), Universidad Autónoma de Coahuila, Facultad de Medicina, Torreón, Coahuila, México.
[Ti] Título:IN VIVO EFFECT OF EXTRACT ON HEPATIC CYTOCHROME 3A1 IN RATS.
[So] Source:Afr J Tradit Complement Altern Med;14(4):62-68, 2017.
[Is] ISSN:2505-0044
[Cp] País de publicação:Nigeria
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Since the time when drugs began to be used, it became evident that they could produce a therapeutic effect, but also a clinical condition of toxicity or no effect at all on humans, despite using the same doses in different patients. Such untoward effects were termed "drug idiosyncrasy" and also "idiosyncratic drug effects", but the factors producing such diverse responses were never taken into account. MATERIALS AND METHODS: L. (fringed rue) is an herbaceous plant of the Rutaceae family used in traditional medicine due to its properties, such as its analgesic and antipyretic effects. This study used 25 male rats divided into five groups. Plant extract was administered to Groups 1 and 2 at doses of 100 and 30 mg/kg/day, respectively, for three days; Group 3 was administered 100 mg/kg/day of dexamethasone (DEX), as well as 100 mg/kg/day of extract; Group 4 was administered 100 mg/kg/day of DEX and treated as positive control; Group 5 was treated as negative control and was administered a physiological solution. Twenty-four hours after the the last dose, the animals were sacrificed and their livers were extracted. RESULTS: The aqueous extract of , intraperitoneally administered, was able to induce cytochrome 3A1 in doses of 30 mg/kg/day, and a greater inducing effect occurs when the plant is co-administered in doses of 100 mg/kg/day with dexamethasone. CONCLUSION: This study suggests that aqueous extract of can induce cytochrome 3a1. This study helps provide a better understanding of CYP3a regulation. Future work is needed to determine the compounds that produce the cytochrome modulation.
[Mh] Termos MeSH primário: Citocromos a3/metabolismo
Fígado/metabolismo
Extratos Vegetais/administração & dosagem
Ruta/química
[Mh] Termos MeSH secundário: Animais
Fígado/efeitos dos fármacos
Masculino
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochromes a3); 0 (Plant Extracts)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.21010/ajtcam.v14i4.8


  2 / 25 MEDLINE  
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[PMID]:28141544
[Au] Autor:Refojo PN; Calisto F; Ribeiro MA; Teixeira M; Pereira MM
[Ad] Endereço:.
[Ti] Título:The monoheme cytochrome c subunit of Alternative Complex III is a direct electron donor to caa3 oxygen reductase in Rhodothermus marinus.
[So] Source:Biol Chem;398(9):1037-1044, 2017 Aug 28.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Alternative Complex III (ACIII) is an example of the robustness and flexibility of prokaryotic respiratory chains. It performs quinol:cytochrome c oxidoreductase activity, being functionally equivalent to the bc1 complex but structurally unrelated. In this work we further explored ACIII investigating the role of its monoheme cytochrome c subunit (ActE). We expressed and characterized the individually isolated ActE, which allowed us to suggest that ActE is a lipoprotein and to show its function as a direct electron donor to the caa3 oxygen reductase.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/química
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Oxirredutases/metabolismo
Subunidades Proteicas/metabolismo
Rhodothermus/enzimologia
[Mh] Termos MeSH secundário: Transporte de Elétrons
Metabolismo dos Lipídeos
Modelos Moleculares
Conformação Proteica
Subunidades Proteicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (Protein Subunits); 0 (cytochrome caa(3)); 9035-34-1 (Cytochromes a); EC 1.- (Oxidoreductases); EC 1.10.2.2 (Electron Transport Complex III)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  3 / 25 MEDLINE  
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[PMID]:25820937
[Au] Autor:Ohta T; Soulimane T; Kitagawa T; Varotsis C
[Ad] Endereço:Graduate School of Life Science, University of Hyogo, Hyogo 678-1297, Japan.
[Ti] Título:Nitric oxide activation by caa3 oxidoreductase from Thermus thermophilus.
[So] Source:Phys Chem Chem Phys;17(16):10894-8, 2015 Apr 28.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Visible and UV-resonance Raman spectroscopy was employed to investigate the reaction of NO with cytochrome caa3 from Thermus thermophilus. We show the formation of the hyponitrite (HO-N=N-O)(-) bound to the heme a3 species (νN=N = 1330 cm(-1)) forming a high spin complex in the oxidized heme a3 Fe/CuB binuclear center of caa3-oxidoreductase. In the absence of heme a3 Fe(2+)-NO formation, the electron required for the formation of the N=N bond originates from the autoreduction of CuB by NO, producing nitrite. With the identification of the hyponitrite intermediate the hypothesis of a common phylogeny of aerobic respiration and bacterial denitrification is fully supported and the mechanism for the 2e(-)/2H(+) reduction of NO to N2O can be described with more certainty.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Óxido Nítrico/metabolismo
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: Heme/metabolismo
Ligantes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (Ligands); 0 (cytochrome caa(3)); 31C4KY9ESH (Nitric Oxide); 42VZT0U6YR (Heme); 9035-34-1 (Cytochromes a)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150409
[Lr] Data última revisão:
150409
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150331
[St] Status:MEDLINE
[do] DOI:10.1039/c5cp01013f


  4 / 25 MEDLINE  
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[PMID]:23399637
[Au] Autor:Noor MR; Soulimane T
[Ad] Endereço:Department of Chemical and Environmental Sciences and Materials and Surface Science Institute (MSSI), University of Limerick, Limerick, Ireland.
[Ti] Título:Structure of caa(3) cytochrome c oxidase--a nature-made enzyme-substrate complex.
[So] Source:Biol Chem;394(5):579-91, 2013 May.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Aerobic respiration, the energetically most favorable metabolic reaction, depends on the action of terminal oxidases that include cytochrome c oxidases. The latter forms a part of the heme-copper oxidase superfamily and consists of three different families (A, B, and C types). The crystal structures of all families have now been determined, allowing a detailed structural comparison from evolutionary and functional perspectives. The A2-type oxidase, exemplified by the Thermus thermophilus caa(3) oxidase, contains the substrate cytochrome c covalently bound to the enzyme complex. In this article, we highlight the various features of caa(3) enzyme and provide a discussion of their importance, including the variations in the proton and electron transfer pathways.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/química
Citocromos a3/química
Citocromos a/química
Complexo IV da Cadeia de Transporte de Elétrons/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Grupo dos Citocromos c/metabolismo
Citocromos a/metabolismo
Citocromos a3/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Modelos Químicos
Dados de Sequência Molecular
Estrutura Molecular
Especificidade por Substrato
Thermus thermophilus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (cytochrome caa(3)); 9035-34-1 (Cytochromes a); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:130424
[Lr] Data última revisão:
130424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130213
[St] Status:MEDLINE


  5 / 25 MEDLINE  
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[PMID]:22763450
[Au] Autor:Lyons JA; Aragão D; Slattery O; Pisliakov AV; Soulimane T; Caffrey M
[Ad] Endereço:Department of Chemical and Environmental Sciences, University of Limerick, Limerick, Ireland.
[Ti] Título:Structural insights into electron transfer in caa3-type cytochrome oxidase.
[So] Source:Nature;487(7408):514-8, 2012 Jul 26.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytochrome c oxidase is a member of the haem copper oxidase superfamily (HCO). HCOs function as the terminal enzymes in the respiratory chain of mitochondria and aerobic prokaryotes, coupling molecular oxygen reduction to transmembrane proton pumping. Integral to the enzyme's function is the transfer of electrons from cytochrome c to the oxidase via a transient association of the two proteins. Electron entry and exit are proposed to occur from the same site on cytochrome c. Here we report the crystal structure of the caa3-type cytochrome oxidase from Thermus thermophilus, which has a covalently tethered cytochrome c domain. Crystals were grown in a bicontinuous mesophase using a synthetic short-chain monoacylglycerol as the hosting lipid. From the electron density map, at 2.36 Å resolution, a novel integral membrane subunit and a native glycoglycerophospholipid embedded in the complex were identified. Contrary to previous electron transfer mechanisms observed for soluble cytochrome c, the structure reveals the architecture of the electron transfer complex for the fused cupredoxin/cytochrome c domain, which implicates different sites on cytochrome c for electron entry and exit. Support for an alternative to the classical proton gate characteristic of this HCO class is presented.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/química
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: Azurina/metabolismo
Domínio Catalítico
Membrana Celular/metabolismo
Cristalização
Cristalografia por Raios X
Transporte de Elétrons
Elétrons
Glicerofosfolipídeos/química
Glicerofosfolipídeos/metabolismo
Modelos Moleculares
Oxigênio/metabolismo
Estrutura Terciária de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Prótons
Água/química
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (Glycerophospholipids); 0 (Protein Subunits); 0 (Protons); 0 (cupredoxin); 0 (cytochrome caa(3)); 059QF0KO0R (Water); 12284-43-4 (Azurin); 9035-34-1 (Cytochromes a); EC 1.9.3.1 (Electron Transport Complex IV); S88TT14065 (Oxygen)
[Em] Mês de entrada:1208
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120706
[St] Status:MEDLINE
[do] DOI:10.1038/nature11182


  6 / 25 MEDLINE  
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[PMID]:21922088
[Au] Autor:Molinas MF; De Candia A; Szajnman SH; Rodríguez JB; Martí M; Pereira M; Teixeira M; Todorovic S; Murgida DH
[Ad] Endereço:Departamento de Química Inorgánica, Analítica y Química Física and INQUIMAE (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pab. 2, piso 1, C1428EHA-Buenos Aires, Argentina.
[Ti] Título:Electron transfer dynamics of Rhodothermus marinus caa3 cytochrome c domains on biomimetic films.
[So] Source:Phys Chem Chem Phys;13(40):18088-98, 2011 Oct 28.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The subunit II of the caa(3) oxygen reductase from Rhodothermus marinus contains, in addition to the Cu(A) center, a c-type heme group in the cytochrome c domain (Cyt-D) that is the putative primary electron acceptor of the enzyme. In this work we have combined surface-enhanced resonance Raman (SERR) spectroelectrochemistry, molecular dynamics (MD) simulations and electron pathway calculations to assess the most likely interaction domains and electron entry/exit points of the truncated Cyt-D of subunit II in the reactions with its electron donor, HiPIP and electron acceptor, Cu(A). The results indicate that the transient interaction between Cyt-D and HiPIP relies upon a delicate balance of hydrophobic and polar contacts for establishing an optimized electron transfer pathway that involves the exposed edge of the heme group and guaranties efficient inter-protein electron transfer on the nanosecond time scale. The reorganization energy of ca. 0.7 eV was determined by time-resolved SERR spectroelectrochemistry. The intramolecular electron transfer pathway in integral subunit II from Cyt-D to the Cu(A) redox center most likely involves the iron ligand histidine 20 as an electron exit point in Cyt-D.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Rhodothermus/enzimologia
[Mh] Termos MeSH secundário: Grupo dos Citocromos c/química
Citocromos a/química
Citocromos a3/química
Transporte de Elétrons
Simulação de Dinâmica Molecular
Estrutura Terciária de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (Protein Subunits); 0 (cytochrome caa(3)); 9035-34-1 (Cytochromes a)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:111005
[Lr] Data última revisão:
111005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110917
[St] Status:MEDLINE
[do] DOI:10.1039/c1cp21925a


  7 / 25 MEDLINE  
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[PMID]:21853973
[Au] Autor:Pavlou A; Soulimane T; Pinakoulaki E
[Ad] Endereço:Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus.
[Ti] Título:Evidence for the presence of two conformations of the heme a3-Cu(B) pocket of cytochrome caa3 from Thermus thermophilus.
[So] Source:J Phys Chem B;115(39):11455-61, 2011 Oct 06.
[Is] ISSN:1520-5207
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Resonance Raman (RR) and "light" minus "dark" Fourier transform infrared (FTIR) difference spectra are reported for the CO-bound caa(3) oxidase from Thermus thermophilus. Two Fe-CO stretching modes at 518 and 507 cm(-1), the Fe-C-O bending mode at 570 cm(-1), and three C-O modes of heme a(3) at 1958, 1967, and 1973 cm(-1) have been identified in the RR and FTIR spectra, respectively. The FTIR "light" minus "dark" spectrum indicates the formation of Cu(B)CO as revealed by its ν(CO) at 2060/2065 cm(-1). We assign the bands at 518 (ν(Fe-CO)) and 1967/1973 cm(-1) (ν(C-O)) as the α-conformation. We also assign the bands at 507 and 1958 cm(-1) (ν(C-O)) as originating from the ß-conformation of the enzyme. A frequency upshift of the heme a(3) Fe-His mode is observed subsequent to CO photolysis from 209 cm(-1) in the equilibrium deoxy enzyme to 214 cm(-1) in the photoproduct. The caa(3) data, distinctly different from those of ba(3) oxidase, are discussed in terms of the coupling of the α- and ß-conformations that occur in heme-copper oxidases with catalytic function. The dynamics between the heme a(3) and heme a propionates as revealed by the perturbation of the bending vibrations δ(prop) of hemes a and a(3) at 385 and 392 cm(-1), respectively, induced upon CO binding to heme a(3) is discussed in terms of the protonic connectivity between the heme a ring-D propionate/Arg site with that of the heme a(3) ring-D propionate-H(2)O site that leads to the highly conserved in the heme-copper oxidases water pool.
[Mh] Termos MeSH primário: Cobre/química
Grupo dos Citocromos c/química
Citocromos a3/química
Citocromos a/química
Heme/análogos & derivados
Thermus thermophilus/química
Thermus thermophilus/metabolismo
[Mh] Termos MeSH secundário: Monóxido de Carbono/química
Domínio Catalítico
Cristalografia por Raios X
Grupo dos Citocromos c/metabolismo
Citocromos a/metabolismo
Citocromos a3/metabolismo
Heme/química
Fotólise
Espectroscopia de Infravermelho com Transformada de Fourier
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (cytochrome caa(3)); 18535-39-2 (heme a); 42VZT0U6YR (Heme); 789U1901C5 (Copper); 7U1EE4V452 (Carbon Monoxide); 9035-34-1 (Cytochromes a)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110823
[St] Status:MEDLINE
[do] DOI:10.1021/jp2033356


  8 / 25 MEDLINE  
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[PMID]:20206595
[Au] Autor:Refojo PN; Teixeira M; Pereira MM
[Ad] Endereço:Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN, 2780-157 Oeiras, Portugal.
[Ti] Título:The alternative complex III of Rhodothermus marinus and its structural and functional association with caa3 oxygen reductase.
[So] Source:Biochim Biophys Acta;1797(8):1477-82, 2010 Aug.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An alternative complex III (ACIII) is a respiratory complex with quinol:electron acceptor oxidoreductase activity. It is the only example of an enzyme performing complex III function that does not belong to bc1 complex family. ACIII from Rhodothermus (R.) marinus was the first enzyme of this type to be isolated and characterized, and in this work we deepen its characterization. We addressed its interaction with quinol substrate and with the caa3 oxygen reductase, whose coding gene cluster follows that of the ACIII. There is at least, one quinone binding site present in R. marinus ACIII as observed by fluorescence quenching titration of HQNO, a quinone analogue inhibitor. Furthermore, electrophoretic and spectroscopic evidences, taken together with mass spectrometry revealed a structural association between ACIII and caa3 oxygen reductase. The association was also shown to be functional, since quinol:oxygen oxidoreductase activity was observed when the two isolated complexes were put together. This work is thus a step forward in the recognition of the structural and functional diversities of prokaryotic respiratory chains.
[Mh] Termos MeSH primário: Grupo dos Citocromos c/química
Citocromos a3/química
Citocromos a/química
Complexo III da Cadeia de Transporte de Elétrons/química
Rhodothermus/metabolismo
[Mh] Termos MeSH secundário: Grupo dos Citocromos c/fisiologia
Citocromos a/fisiologia
Citocromos a3/fisiologia
Complexo III da Cadeia de Transporte de Elétrons/genética
Complexo III da Cadeia de Transporte de Elétrons/fisiologia
Fluorescência
Família Multigênica
Vitamina K/análogos & derivados
Vitamina K/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (cytochrome caa(3)); 12001-79-5 (Vitamin K); 9035-34-1 (Cytochromes a); EC 1.10.2.2 (Electron Transport Complex III); VQ093653DO (menadiol)
[Em] Mês de entrada:1008
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100309
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbabio.2010.02.029


  9 / 25 MEDLINE  
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[PMID]:18676644
[Au] Autor:Veríssimo AF; Sousa FL; Baptista AM; Teixeira M; Pereira MM
[Ad] Endereço:Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
[Ti] Título:Thermodynamic redox behavior of the heme centers in A-type heme-copper oxygen reductases: comparison between the two subfamilies.
[So] Source:Biophys J;95(9):4448-55, 2008 Nov 01.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The study of the thermodynamic redox behavior of the hemes from two members of the A family of heme-copper oxygen reductases, Paracoccus denitrificans aa3 (A1 subfamily) and Rhodothermus marinus caa3 (A2 subfamily) enzymes, is presented. At different pH values, midpoint reduction potentials and interaction potentials were obtained in the framework of a pairwise model for two interacting redox centers. In both enzymes, the hemes have different reduction potentials. For the A1-type enzyme, it was shown that heme a has a pH-dependent midpoint reduction potential, whereas that of heme a3 is pH independent. For the A2-type enzyme the opposite was observed. The midpoint reduction potential of heme c from subunit II of the caa3 enzyme was determined by fitting the data with a single-electron Nernst curve, and it was shown to be pH dependent. The results presented here for these A-type enzymes are compared with those previously obtained for representative members of the B and C families.
[Mh] Termos MeSH primário: Cobre/metabolismo
Grupo dos Citocromos c/metabolismo
Citocromos a3/metabolismo
Citocromos a/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Heme/metabolismo
Paracoccus denitrificans/enzimologia
Rhodothermus/enzimologia
[Mh] Termos MeSH secundário: Grupo dos Citocromos c/química
Citocromos a/química
Citocromos a3/química
Complexo IV da Cadeia de Transporte de Elétrons/química
Concentração de Íons de Hidrogênio
Oxirredução
Análise Espectral
Termodinâmica
Titulometria
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (cytochrome caa(3)); 42VZT0U6YR (Heme); 789U1901C5 (Copper); 9035-34-1 (Cytochromes a); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:0812
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080805
[St] Status:MEDLINE
[do] DOI:10.1529/biophysj.108.139493


  10 / 25 MEDLINE  
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[PMID]:18294138
[Au] Autor:Muntyan MS; Bloch DA
[Ad] Endereço:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. muntyan@genebee.msu.su
[Ti] Título:Study of redox potential in cytochrome c covalently bound to terminal oxidase of alkaliphilic Bacillus pseudofirmus FTU.
[So] Source:Biochemistry (Mosc);73(1):107-11, 2008 Jan.
[Is] ISSN:0006-2979
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Spectroelectrochemistry was used to determine the midpoint redox potentials of heme cofactors of the caa3-type cytochrome oxidase from the alkaliphilic bacterium Bacillus pseudofirmus FTU. The apparent midpoint potentials (E(m)(app)) for the most prominent transitions of hemes a and a3 (+193 and +334 mV, respectively) were found to be similar to the values reported for other enzymes with high homology to the caa3-type oxidase. In contrast, the midpoint potential of the covalently bound cytochrome c (+89 mV) was 150-170 mV lower than in cytochromes c, either low molecular weight or covalently bound to the caa3 complex in all known aerobic neutralophilic and thermo-neutralophilic bacteria. Such an unusually low redox potential of the covalently bound cytochrome c of the caa3-type oxidase of alkaliphilic bacteria, together with high redox potentials of hemes a and a3, ensures more than twice higher difference in redox potentials inside the respiratory complex compared to the homologous mitochondrial enzyme. The energy released during this redox transition might be stored in the transmembrane H+ gradient even under low Deltap in the alkaline environment of the bacteria at the expense of a significant increase in DeltaG of the coupled redox reaction.
[Mh] Termos MeSH primário: Bacillus/enzimologia
Grupo dos Citocromos c/química
Citocromos a3/química
Citocromos a/química
Complexo IV da Cadeia de Transporte de Elétrons/química
[Mh] Termos MeSH secundário: Oxirredução
Potenciometria
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome c Group); 0 (Cytochromes a3); 0 (cytochrome caa(3)); 9035-34-1 (Cytochromes a); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:0806
[Cu] Atualização por classe:080225
[Lr] Data última revisão:
080225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080226
[St] Status:MEDLINE



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