TY - JOUR. T1 - Low levels of ATP synthase and cytochrome c oxidase subunit peptide from hearts of copper-deficient rats are not altered by the administration of dimethyl sulfoxide. AU - Chao, J. C J. AU - Medeiros, D. M.. AU - Davidson, J.. AU - Shiry, L.. PY - 1994. Y1 - 1994. N2 - This study determined if reported decreases in the δ subunit of ATP synthase and nuclear-encoded cytochrome c oxidase subunits in hearts of copper-deficient rats were secondary to the heart disease pathology or due to lack of the trace element. Male weanling Long-Evans rats were randomly divided into six groups: rats fed a copper-adequate or copper-deficient diet (with free access) with or without 5% dimethyl sulfoxide (DMSO) in the drinking water and rats pair-fed the copper-adequate or copper-deficient diet without DMSO treatment. After 4 wk, rats in the groups fed the copper- deficient diet had lower liver superoxide dismutase and heart cytochrome c oxidase activities compared with groups fed the copper-adequate ...
AS04 052, anti-Cytochrome COXII oxidase subunit II respiration respiratory chain antibody , cytochrome oxidase subunit II, plant COXII antibody, marker antibody for plant mitochondria, P04373. Q1XGA9, AtmG00160
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Copper atom in PDB 2ein: Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State
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Heme A is an obligatory cofactor in eukaryotic cytochrome c oxidase (CcO), but little is known about how heme A is inserted into CcO, or how the flux of heme th...
Article Pet191 is a cytochrome c oxidase assembly factor in saccharomyces cerevisiae. The twin-Cx9C motif protein Pet191 is essential for cytochrome c oxidase maturation. The motif Cys residues are functionally important and appear to be present in d...
Cytochrome c oxidase was isolated from human hearts and separated by SDS gel electrophoresis. The identity of polypeptide bands with known subunits was demonstrated by immunoblotting with monospecific antisera to rat liver cytochrome c oxidase subunits. The polarographically determined kinetics of cytochrome c oxidation were similar to those reported for the bovine heart enzyme.
Top performende anti-Human SCO1 Cytochrome C Oxidase Assembly Protein Antikörper für Immunohistochemistry (IHC) vergleichen & kaufen.
Cytochrome C oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit Vb of the human mitochondrial respiratory chain enzyme. [provided by RefSeq, Jul 2008 ...
The hypothesis explains the molecular basis for restoring mitochondrial function by laser therapy. It also explains how laser therapy reverses both excessive oxidation (lack of NADH/FADH2) and excessive reduction (lack of O2) states of cytochrome c oxidase complex. It is proposed that photons interact with heme molecules of cytochrome c oxidase. A molecule of heme contains a porphyrin ring and an atom of iron in the center. The iron atom (Fe) can switch oxidation states back and forth between ferrous (Fe2+) and ferric (Fe3+) by accepting or releasing an electron. The porphyrin ring is a complex aromatic molecule that has 26 pi electrons which are "delocalized", spinning in the carbon rings creating a resonating electromagnetic cloud. Photons with similar wavelengths are absorbed by the cloud increasing its energy. The energy is then passed on to the centrally located atom of iron existing in a reduced state (Fe2+). The electrons on the orbits of the iron atom accept this electromagnetic energy, ...
C57BL/6J mice were fed under four different experimental conditions for 17 weeks: normal diet (ND), high fat diet (HFD), HFD with 5% RJ, and HFD with 5% honey bee larva powder (BL). Spontaneous locomotor activity, hepatic triglyceride (TG) content, and blood parameters were examined. Gene and protein expressions of thermogenic uncoupling protein 1 (UCP1) and mitochondrial cytochrome c oxidase subunit IV (COX-IV) in BAT and WAT were investigated by qPCR and Western blotting analysis, respectively ...
The mitochondrial cytochrome c oxidase (complex IV; COX) of the respiratory chain transfers electrons from cytochrome c to oxygen. The activity of the respiratory chain complexes generates a proton-gradient across the inner membrane, which is used by the ATP-synthase to produce ATP for cellular metabolism. In baker´s yeast Saccharomyces cerevisiae complex IV forms a supercomplex with cytochrome c reductase (complex III, bc1) and consists of eight nuclear-encoded and three mitochondrially-encoded subunits. The formation of complex IV is crucial for respiratory growth. The translocase of the outer membrane (TOM complex) imports precursors of nuclear-encoded COX subunits into mitochondria. Subsequently, the presequence translocase (TIM23 complex) transports the majority of these precursor proteins into or across the inner membrane in a membrane potential dependent manner. The presequence translocase-associated motor (PAM) drives the translocation into the mitochondrial matrix. The ATPase activity ...
MIRICPIVRS KVPLLGTFLR SDSWLAPHAL ALRRAICKNV ALRSYSVNSE QPKHTFDISK LTRNEIQQLR ELKRARERKF KDRTVAFYFS SVAVLFLGLA YAAVPLYRAI CARTGFGGIP ITDRRKFTDD KLIPVDTEKR IRISFTSEVS QILPWKFVPQ QREVYVLPGE TALAFYKAKN YSDKDIIGMA TYSIAPGEAA QYFNKIQCFC FEEQKLAAGE EIDMPVFFFI DPDFASDPAM RNIDDIILHY TFFRAHYGDG TAVSDSKKEP EMNADEKAAS LANAAILSPE VIDTRKDNSN ...
Cytochrome c oxidase is the terminal enzyme in the respiratory chains of mitochondria and many bacteria where it translocates protons across a membrane thereby maintaining an electrochemical proton gradient. Results from earlier studies on detergent-solubilized cytochrome c oxidase have shown that individual reaction steps associated with proton pumping display pH-dependent kinetics. Here, we investigated the effect of pH on the kinetics of these reaction steps with membrane-reconstituted cytochrome c oxidase such that the pH was adjusted to different values on the inside and outside of the membrane. The results show that the pH on the inside of the membrane fully determines the kinetics of internal electron transfers that are linked to proton pumping. Thus, even though proton release is rate limiting for these reaction steps (Salomonsson et al., Proc. Natl. Acad. Sci. USA, 2005, 102, 17624), the transition kinetics is insensitive to the outside pH (in the range 6-9.5).. ...
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Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
Introduction: The PCR-based analysis of homologous genes has become one of the most powerful approaches for species detection and identification, particularly with the recent availability of Next Generation Sequencing platforms (NGS) making it possible to identify species composition from a broad range of environmental samples. Identifying species from these samples relies on the ability to match sequences with reference barcodes for taxonomic identification. Unfortunately, most studies of environmental samples have targeted ribosomal markers, despite the fact that the mitochondrial Cytochrome c Oxidase subunit I gene (COI) is by far the most widely available sequence region in public reference libraries. This is largely because the available versatile ("universal") COI primers target the 658 barcoding region, whose size is considered too large for many NGS applications. Moreover, traditional barcoding primers are known to be poorly conserved across some taxonomic groups. Results: We first ...
Four Donax species, D. semistriatus, D. trunculus, D. variegatus and D. vittatus, are found on European coasts. Nevertheless, despite their economic importance there is not a reliable method to differ
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Aerobic organisms derive energy needed to sustain life from foodstuffs through the process of cellular respiration. Respiration is performed by a series of soluble and multi-subunit membrane proteins that form the electron-transport chain, found in the inner mitochondrial membrane of eukaryotes and the cytoplasmic membrane of aerobic prokaryotes. Cytochrome c oxidase, the terminal member of this respiratory chain, catalyzes the four-electron reduction of oxygen to water and uses the free energy of this reaction to translocates protons across the membrane. The oxidase accomplishes oxygen reduction by drawing electron and protons from the opposite sides of the membrane and transfers the pumped protons against the membrane potential through very specific routes within the enzyme. Several years of research have thrown some light on the electron and the proton-input pathways, catalytic cycle intermediates and the timing of the proton-pumping steps. However, the coupling of the oxygen chemistry to ...
The organization of cells in different compartments demands specific mechanisms to supply each organelle with its proper subset of proteins. While it is already known that presequences in precursor proteins contain the information which guides these proteins to their correct organelle, very little is known about the mechanism of the transmembrane movement of proteins. We have studied the mechanism of protein transport into mitochondria using an artificial mitochondrial precursor protein containing the cytosolic enzyme mouse dihydrofolate reductase (DHFR) fused to the presequence of yeast cytochrome oxidase subunit IV (coxIV). This precursor (coxIV-DHFR) can be imported into mitochondria in vitro as well as in vivo [ l ] and can be purified in its native form after over-expression in Escherichiu coli [2]. This precursor was modified so that it would get stuck in the import pathway and thereby provide a tool to identify molecular components of the translocation machinery. Using the same approach, we
Cytochrome-c-oxidase immunohistochemistry in the liver. (A) The subunit II/III lacks in most of the hepatocytes but is retained in the biliary ducts (↑). (B)
Adkins, R. M. and R. L. Honeycutt. 1994. Evolution of the primate cytochrome c oxidase subunit II gene. Journal of Molecular Evolution 38:215-231.. Arnason, U., A. Gullberg, and A. Janke. 1998. Molecular timing of primate divergences as estimated by two nonprimate calibration points. Journal of Molecular Evolution 47:718-727.. Bailey, W. J., D. H. A. Fitch, D. A. Tagle, J. Czelusniak, J. L. Slightom, and M. Goodman. 1991. Molecular evolution of the PSI-eta-globin gene locus: Gibbon phylogeny and the hominoid slowdown. Molecular Biology and Evolution 8:155-184.. Barton, R. A. 2004. Binocularity and brain evolution in primates. Proceedings of the National Academy of Sciences (USA) 101(27):10113-10115.. Bloch, J. I. and D. M. Boyer. 2002. Grasping primate origins. Science298:1606-1610.. Bloch, J. I., D. C. Fisher, P. D. Gingerich, G. F. Gunnell, E. L. Simons, and M. D. Uhen. 1997. Cladistic analysis and anthropoid origins. Science 278:2134-2135.. Fleagle, J. G. 1999. Primate Adaptation and ...
T. Zhu, S. Faulkner, T. Madaan, A. Bainbridge, D. Price, D. Thomas, E. Cady, N. Robertson, X. Golay, and I. Tachtsidis, "Optimal Wavelength Combinations for Resolving in-vivo Changes of Haemoglobin and Cytochrome-c-oxidase Concentrations with NIRS," in Biomedical Optics and 3-D Imaging, OSA Technical Digest (Optical Society of America, 2012), paper JM3A.6 ...
COX6B1 - COX6B1 (Myc-DDK-tagged)-Human cytochrome c oxidase subunit VIb polypeptide 1 (ubiquitous) (COX6B1), nuclear gene encoding mitochondrial protein available for purchase from OriGene - Your Gene Company.
Cytochrome c oxidase subunit 6C is an enzyme that in humans is encoded by the COX6C gene.[4][5] Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. This nuclear gene encodes subunit VIc, which has 77% amino acid sequence identity with mouse COX subunit VIc. This gene is up-regulated in prostate cancer cells. A pseudogene COX6CP1 has been found on chromosomes 16p12.[5] ...
Nitric oxide (NO) has been implicated in several cellular processes as a signaling molecule and also as a source of reactive nitrogen species (RNS). NO is produced by three isoenzymes called nitric oxide synthases (NOS), all present in skeletal muscle. While neuronal NOS (nNOS) and endothelial NOS (eNOS) are isoforms constitutively expressed, inducible NOS (iNOS) is mainly expressed during inflammatory responses. Recent studies have demonstrated that NO is also involved in the mitochondrial biogenesis pathway, having PGC-1α as the main signaling molecule. Increased NO synthesis has been demonstrated in the sarcolemma of skeletal muscle fiber and NO can also reversibly inhibit cytochrome c oxidase (Complex IV of the respiratory chain). Investigation on cultured skeletal myotubes treated with NO donors, NO precursors or NOS inhibitors have also showed a bimodal effect of NO that depends on the concentration used. The present review will discuss the new insights on NO roles on mitochondrial biogenesis and
Epidermal growth factor receptor (EGFR) and nonreceptor tyrosine kinase c-Src, whose combined overexpression occurs in some breast cancers, cooperate to promote transformed characteristics when overexpressed in fibroblasts. Their synergistic interaction, which depends on c-Src phosphorylation of EGFR tyrosine 845 (pY845), is independent of EGFR kinase activity and of its activation of the mitogen-associated protein kinase signaling pathway. Boerner et al. screened a phage display library with a peptide corresponding to the region of EGFR that contains pY845 and identified cytochrome c oxidase subunit II (CoxII) as a binding partner. In mouse fibroblasts overexpressing EGFR and c-Src and in a breast cancer cell line that overexpresses both EGFR and c-Src, CoxII coimmunoprecipitated with EGFR. Coimmunoprecipitation, which was enhanced by EGF treatment, did not occur with overexpression of a catalytically inactive c-Src mutant or when Y845 was replaced by phenylalanine (Y845F-EGFR). The authors ...
Endogenous nitric oxide (NO) acts on cytochrome c oxidase, the terminal enzyme in the mitochondrial electron transport chain, inhibiting mitochondrial oxygen consumption and promoting the release of free radicals. Quintero et al. investigated the consequences of NO regulation of mitochondrial activity in vascular endothelial cells, which are highly glycolytic and have abundant NO. Analysis of the effects of inhibitors of mitochondrial electron transport or glycolysis at various oxygen concentrations indicated that ATP production in human umbilical vein endothelial cells (HUVECs) depended more on glycolysis than it did on mitochondrial respiration. Exposure to a low concentration of oxygen (1.5%) that promoted the accumulation of hypoxia-inducible factor 1α (HIF-1α) in human smooth muscle and epithelial kidney cells had little effect on HIF-1α abundance in human vascular endothelial cells unless the production of NO was inhibited. The ability of NO to inhibit HIF-1α accumulation in HUVECs ...
Cytochrome c oxidase subunit I (CO1 or MTCO1) is 1 of 3 mitochondrial DNA (mtDNA) encoded subunits (MTCO1, MTCO2, MTCO3) of respiratory Complex IV.…
Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (551 aa ...
Weve investigated the consequences of hypoxia and myocardial ischemia/reperfusion for the framework and function of cytochrome oxidase (CcO). immunoprecipitated CcO complicated. Most oddly enough, both H89 and MPI put into the perfusion moderate dramatically decreased the ischemia/reperfusion problems for the myocardial cells. Our results directed to a thrilling chance for using CcO activity modulators for managing myocardial damage connected with ischemia and oxidative tension circumstances. 404950-80-7 Cytochrome oxidase (CcO)3 may be the terminal oxidase from the mitochondrial 404950-80-7 electron transportation string, whose activity is normally modulated in response to O2 stress and the task load from the tissues (1-6). This rate-limiting enzyme can be an essential site of legislation of mitochondrial respiration and oxidative phosphorylation (7). In the 404950-80-7 SCA12 fungus, changed CcO activity in response to aerobic and anaerobic circumstances is from the differential appearance of ...
In this section, a culture of HeLa cells that was transfected with a pEYFP-Mitochondria plasmid subcellular localization vector, which contains the mitochondrial targeting sequence from subunit VIII of human cytochrome C oxidase, is featured.
Buy Kinetic and Mechanistic Studies on Cytochrome P450-Related High-Valent Porphyrin-Iron-Oxo Species by Zhengzheng Pan from Waterstones today! Click and Collect from your local Waterstones or get FREE UK delivery on orders over £20.
A phylogeny was reconstructed for four species belonging to the Neotropical Anopheles (Nyssorhynchus) albitarsis complex using partial sequences from the mitochondrial cytochrome oxidase I (COI) and NADH dehydrogenase 4 (ND4) genes and the ribosomal DNA ITS2 and D2 expansion region of the 28S subunit. The basis for initial characterization of each member of the complex was by correlated random amp ...
Tissue processing and data analysis. Frozen sections were cut on a sliding microtome at 31 μm for horizontal material and at 50 μm for tangential material. Sections were collected in phosphate buffer (0.1 m) and were processed immediately for HRP using the TMB method of Mesulam et al. (1978; see Felleman et al., 1996). Sections containing fluorescent, retrogradely labeled cells were mounted on glass slides from 0.05 m phosphate buffer and air dried before observation under UV epifluorescence using a Zeiss Axiophot microscope. Alternative sections were processed for cytochrome oxidase histochemistry according to the protocol of Wong-Riley and Carroll (1984). The myeloarchitectonic borders of V3, MT, and floor of the superior temporal sulcus area (FST) were determined from sections stained according to the protocol of Gallyas (1979) in 5 of 10 PITv injection cases.. A computer-interfaced microscope system (Neurolucida) was used to record the positions of labeled cells, axon terminals, borders of ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Kazumasa Muramoto, Hirohito Terada, Tsuyoshi Kurauchi, Yoshiki Tadehara, Akiko Yamasaki, Takashi Sugimura, Sadamu Kurono, Kazuo Tsujimoto, Tsunehiro Mizushima, Eiki Yamashita, Tomitake Structures and physiological roles of all the integral lipids of bovine heart cytochrome c oxidase.. EMBO J. 26, 1713-1725, (2007).[Pub Med]. ...
The metabolic control of respiration is still poorly understood, due mainly to the lack of suitable approaches for studying it in vivo. Experiments on isolated mammalian mitochondria have indicated that a relatively small fraction of each of several components of the electron transport chain is sufficient to sustain a normal O-2 consumption rate. These experiments, however, may not reflect accurately the in vivo situation, due to the lack in the mitochondrial fraction of essential cytosolic components and to the use of excess of substrates in the in vitro assays. An approach is described here whereby the control of respiration by cytochrome c oxidase (COX; EC 1.9.3.1) was analyzed in intact cultured human osteosarcoma 143B.TK- cells and other wild-type cells and in mitochondrial DNA mutation-carrying human cell lines. Surprisingly, in wild-type cells, only a slightly higher COX capacity mas detected than required to support the endogenous respiration rate, pointing to a tighter in vivo control ...
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In the current analysis Cytochrome c oxidase subunit I (CO1 or MT-CO1) protein sequence from GWD has been used to study the MHC binding antigenic peptide, antigenic pepti..
Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (513 aa ...
Homo sapiens COX17 homolog, cytochrome c oxidase assembly protein (yeast) (COX17), nuclear gene encoding mitochondrial protein, mRNA. (H00010063-R01) - Products - Abnova
Complete information for COX20 gene (Protein Coding), COX20, Cytochrome C Oxidase Assembly Factor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for COX7A2L gene (Protein Coding), Cytochrome C Oxidase Subunit 7A2 Like, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
CP000247.PE483 Location/Qualifiers FT CDS complement(515274..515888) FT /codon_start=1 FT /transl_table=11 FT /locus_tag="ECP_0490" FT /product="cytochrome O ubiquinol oxidase subunit III" FT /EC_number="1.10.3.-" FT /db_xref="EnsemblGenomes-Gn:ECP_0490" FT /db_xref="EnsemblGenomes-Tr:ABG68519" FT /db_xref="GOA:A0A454A1T2" FT /db_xref="InterPro:IPR000298" FT /db_xref="InterPro:IPR013833" FT /db_xref="InterPro:IPR014206" FT /db_xref="InterPro:IPR024791" FT /db_xref="InterPro:IPR033946" FT /db_xref="InterPro:IPR035973" FT /db_xref="UniProtKB/TrEMBL:A0A454A1T2" FT /protein_id="ABG68519.1" FT /translation="MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFA FT TYAVLVNGTAGGPTGKDIFELPFVLVETFFLLFSSITYGMAAIAMYKNNKSQVISWLAL FT TWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQ FT IARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM" MATDTLTHAT AHAHEHGHHD AGGTKIFGFW IYLMSDCILF SILFATYAVL VNGTAGGPTG 60 KDIFELPFVL VETFFLLFSS ITYGMAAIAM YKNNKSQVIS WLALTWLFGA GFIGMEIYEF 120 HHLIVNGMGP DRSGFLSAFF ALVGTHGLHV TSGLIWMAVL ...
COX7B2 antibody [N1C3] (cytochrome c oxidase subunit VIIb2) for ICC/IF, IHC-P, WB. Anti-COX7B2 pAb (GTX110995) is tested in Human samples. 100% Ab-Assurance.
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