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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


  2 / 32 MEDLINE  
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[PMID]:26041781
[Au] Autor:Li TF; Painter RG; Ban B; Blake RC
[Ad] Endereço:From the College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125.
[Ti] Título:The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant.
[So] Source:J Biol Chem;290(30):18293-303, 2015 Jul 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Electron transfer reactions among three prominent colored proteins in intact cells of Acidithiobacillus ferrooxidans were monitored using an integrating cavity absorption meter that permitted the acquisition of accurate absorbance data in suspensions of cells that scattered light. The concentrations of proteins in the periplasmic space were estimated to be 350 and 25 mg/ml for rusticyanin and cytochrome c, respectively; cytochrome a was present as one molecule for every 91 nm(2) in the cytoplasmic membrane. All three proteins were rapidly reduced to the same relative extent when suspensions of live bacteria were mixed with different concentrations of ferrous ions at pH 1.5. The subsequent molecular oxygen-dependent oxidation of the multicenter respiratory chain occurred with a single macroscopic rate constant, regardless of the proteins' in vitro redox potentials or their putative positions in the aerobic iron respiratory chain. The crowded electron transport proteins in the periplasm of the organism constituted an electron conductive medium where the network of protein interactions functioned in a concerted fashion as a single ensemble with a standard reduction potential of 650 mV. The appearance of product ferric ions was correlated with the reduction levels of the periplasmic electron transfer proteins; the limiting first-order catalytic rate constant for aerobic respiration on iron was 7,400 s(-1). The ability to conduct direct spectrophotometric studies under noninvasive physiological conditions represents a new and powerful approach to examine the extent and rates of biological events in situ without disrupting the complexity of the live cellular environment.
[Mh] Termos MeSH primário: Acidithiobacillus/metabolismo
Transporte de Elétrons
Ferro/metabolismo
Oxirredução
[Mh] Termos MeSH secundário: Acidithiobacillus/química
Aerobiose
Citocromos a/metabolismo
Citocromos c/metabolismo
Ferro/química
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
9007-43-6 (Cytochromes c); 9035-34-1 (Cytochromes a); E1UOL152H7 (Iron)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150605
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.657551


  3 / 32 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 / 32 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 / 32 MEDLINE  
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[PMID]:23099666
[Au] Autor:Pokkuluri PR; Yang X; Londer YY; Schiffer M
[Ad] Endereço:Biosciences Division, Argonne National Laboratory, Lemont, IL 60439, USA.
[Ti] Título:Pitfalls in the interpretation of structural changes in mutant proteins from crystal structures.
[So] Source:J Struct Funct Genomics;13(4):227-32, 2012 Dec.
[Is] ISSN:1570-0267
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:PpcA is a small protein with 71 residues that contains three covalently bound hemes. The structures of single mutants at residue 58 have shown larger deviations in another part of the protein molecule than at the site of the mutation. Closer examination of the crystal packing has revealed the origin of this unexpected structural change. The site of mutation is within Van der Waals distance from another protein molecule related by a crystallographic twofold axis within the crystal. The structural changes occurred at or near the mutation site have led to a slight adjustment of the surface residues in contact. The observed deviations between the native and the mutant molecular structures are derived from the new crystal packing even though the two crystals are essentially isomorphous. Without careful consideration of the crystal lattice a non-expert looking at only the coordinates deposited in the Protein Data Bank could draw erroneous conclusion that mutation in one part of the molecule affected the structure of the protein in a distant part of the molecule.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Citocromos a/química
Geobacter/química
Proteínas Mutantes/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Cristalografia por Raios X/métodos
Citocromos a/genética
Bases de Dados de Proteínas
Escherichia coli/química
Escherichia coli/genética
Geobacter/genética
Modelos Moleculares
Mutagênese Sítio-Dirigida
Proteínas Mutantes/genética
Mutação
Periplasma/química
Periplasma/genética
Conformação Proteica
Proteômica/métodos
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Mutant Proteins); 9035-34-1 (Cytochromes a)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121027
[St] Status:MEDLINE
[do] DOI:10.1007/s10969-012-9147-1


  6 / 32 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


  7 / 32 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


  8 / 32 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


  9 / 32 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


  10 / 32 MEDLINE  
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[PMID]:19751739
[Au] Autor:Yeh ST; Lee HL; Aune SE; Chen CL; Chen YR; Angelos MG
[Ad] Endereço:Davis Heart and Lung Research Institute, The Ohio State University, Columbus, OH 43210, USA; Department of Emergency Medicine, The Ohio State University, Columbus, OH 43210, USA; Biophysics Graduate Program, The Ohio State University, Columbus, OH 43210, USA.
[Ti] Título:Preservation of mitochondrial function with cardiopulmonary resuscitation in prolonged cardiac arrest in rats.
[So] Source:J Mol Cell Cardiol;47(6):789-97, 2009 Dec.
[Is] ISSN:1095-8584
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:During cardiac arrest (CA), myocardial perfusion is solely dependent on cardiopulmonary resuscitation (CPR) although closed-chest compressions only provide about 10-20% of normal myocardial perfusion. The study was conducted in a whole animal CPR model to determine whether CPR-generated oxygen delivery preserves or worsens mitochondrial function. Male Sprague-Dawley rats (400-450 g) were randomly divided into four groups: (1) BL (instrumentation only, no cardiac arrest), (2) CA(15) (15 min cardiac arrest without CPR), (3) CA(25) (25 min cardiac arrest without CPR) and (4) CPR (15 min cardiac arrest, followed by 10 min CPR). The differences between groups were evaluated by measuring mitochondrial respiration, electron transport chain (ETC) complex activities and mitochondrial ultrastructure by transmission electron microscopy (TEM). The CA(25) group had the greatest impairment of mitochondrial respiration and ETC complex activities (I-III). In contrast, the CPR group was not different from the CA(15) group regarding all measures of mitochondrial function. Complex I was more susceptible to ischemic injury than the other complexes and was the major determinant of mitochondrial dysfunction. Observations of mitochondrial ultrastructure by TEM were compatible with the biochemical results. The findings suggest that, despite low blood flow and oxygen delivery, CPR is able to preserve heart mitochondrial function and viability during ongoing global ischemia. Preservation of complex I activity and mitochondrial function during cardiac arrest may be an important mechanism underlying the beneficial effects of CPR which have been shown in clinical studies.
[Mh] Termos MeSH primário: Reanimação Cardiopulmonar
Parada Cardíaca/fisiopatologia
Mitocôndrias Cardíacas/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Respiração Celular
Citocromos a/metabolismo
Densitometria
Transporte de Elétrons
Parada Cardíaca/patologia
Masculino
Mitocôndrias Cardíacas/ultraestrutura
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9035-34-1 (Cytochromes a)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:161122
[Lr] Data última revisão:
161122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090916
[St] Status:MEDLINE
[do] DOI:10.1016/j.yjmcc.2009.09.003



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