PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23984829-11 2014 Path analysis indicated that number of atoms, oxygen & nitrogen atoms, and Log P are the greatest determinants for formula weight for known COX-2 inhibitors. Nitrogen 59-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-149 24594722-4 2014 Each 2,5-PDC(2-) anion chelates to one Co(II) cation via the pyridine N atom and an O atom of the adjacent carboxylate group, and links to two other Co(II) cations in a bridging mode via the O atoms of the other carboxylate group. Nitrogen 70-71 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 23884539-0 2013 Employing tripodal carboxylate ligand to construct Co(II) coordination networks modulated by N-donor ligands: syntheses, structures and magnetic properties. Nitrogen 93-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-56 23435550-0 2013 First structurally characterized self-assembly of bipodal N-thiophosphorylated bis-thiourea with Co(II): magnetic properties and thermal decomposition. Nitrogen 58-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 23508268-4 2013 The tbta ligand binds to the Co(II) centers through the three triazole nitrogen donor atoms in a facial form, with the Co-N(amine) distance of 2.494(2) A acting as a capping bond to the octahedron. Nitrogen 71-79 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 22354161-2 2012 Single crystal X-ray diffraction studies revealed that the Co(II) complex, {[Co(H(2)L)(H(2)O)(2)](NO(3))(2) 3H(2)O}(n) has a slightly distorted octahedral geometry around the central Co(II) ion; the ligand is coordinated through the ONO donor atoms to one Co(II) metal center and bridged through the pyridine nitrogen atom to another similar Co(II) center so as to form a one-dimensional polymeric unit. Nitrogen 309-317 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 23634005-1 2013 In the title compound, [Co(C7H4ClO2)2(C5H5N)2(H2O)], the Co(II) atom is six-coordinated by three O atoms from a bidentate and a monodentate 4-chloro-benzoate ligand, two N atoms from two pyridine ligands and a water O atom, giving a distorted octa-hedral geometry. Nitrogen 42-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 23398593-10 2013 The desolvated Co(II)(pybz)2 can absorb several gases such as CO2, N2, H2, and CH4 and also vapors of methanol, ethanol, benzene, and cyclohexane. Nitrogen 67-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 23125582-1 2012 In the title compound, [Co(CH(3)CO(2))(C(18)H(24)N(6))]PF(6), the Co(II) atom is penta-coordinated in a distorted trigonal-bipyramidal geometry by four N atoms from a tripodal ligand and one O atom from a monodentate acetate ligand. Nitrogen 49-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 22904774-1 2012 In the title polymeric complex, [Co(NCS)(2){SC(NH(2))(2)}(2)](n), the asymmetric unit comprises a Co(II) ion, which is situated on an inversion centre, an N-bound thio-cyanate anion and a mu(2)-bridging thio-urea mol-ecule. Nitrogen 36-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 98-104 22301678-8 2012 The former Co(II) complexes revealed a six-coordinate octahedron with one amine nitrogen, three pyridyl nitrogens, and two counter anions, and one coordinated anion, Cl(-), Br(-) and N(3)(-), forming intramolecular hydrogen bonds with two pivalamide N-H groups. Nitrogen 80-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 22301678-8 2012 The former Co(II) complexes revealed a six-coordinate octahedron with one amine nitrogen, three pyridyl nitrogens, and two counter anions, and one coordinated anion, Cl(-), Br(-) and N(3)(-), forming intramolecular hydrogen bonds with two pivalamide N-H groups. Nitrogen 104-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 22301678-9 2012 On the other hand, the latter Co(II) complexes showed a seven-coordinate face-capped octahedron with one amine nitrogen, three pyridyl nitrogens, two pivalamide carbonyl oxygens and MeCN or MeOH. Nitrogen 111-119 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 22301678-9 2012 On the other hand, the latter Co(II) complexes showed a seven-coordinate face-capped octahedron with one amine nitrogen, three pyridyl nitrogens, two pivalamide carbonyl oxygens and MeCN or MeOH. Nitrogen 135-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 22361134-5 2012 Molecular modeling studies employing compound 20 showed that the phenyl CF(3) substituent attached to the CN spacer is positioned near the secondary pocket of the COX-2 active site, the CN nitrogen atom is hydrogen bonded (N NH=2.85 A) to the H90 residue, and the indole N-1 benzoyl is positioned in a hydrophobic pocket of the COX-2 active site near W387. Nitrogen 189-197 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-168 22411760-2 2012 The resulting PANI/SBA-15 is capable of chelating Co(II) ions, presumably via its nitrogen atoms on PANI/diamine groups. Nitrogen 82-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 21754669-1 2011 In the title compound, [Co(NO(3))(2)(C(18)H(16)N(2)O(2))(2)](n), the Co(II) ion is located on an inversion center and is six-coordinated in an octa-hedral environment defined by four N atoms of the pyridine rings and two O atoms of the nitrate anions. Nitrogen 27-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 21866283-1 2011 The monoanionic N(4)O ligand N-methyl-N,N"-bis(2-pyridylmethyl)ethylenediamine-N"-acetate (mebpena(-)) undergoes oxidative C-N bond cleavage in the presence of Co(II) and O(2). Nitrogen 16-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 160-166 21913670-2 2011 The Co(II) complexes generally adopt a tetrahedral configuration of general formula [(NP2)Co(I)(2)], wherein the two phosphorus donors are bound to the metal center but the central N-donor remains unbound. Nitrogen 86-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21986896-2 2011 Compound 1 is a polymer in which ligand L coordinates to tetrahedral Co(II) ions in a bidentate bridging fashion using the pyridine nitrogen and carbonyl oxygen atoms. Nitrogen 132-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 21890358-3 2011 Molecular modeling studies for 9f showed that the SO(2)NH(2) group assumes a position within the secondary pocket of the COX-2 active site wherein the SO(2)NH(2) oxygen atom is hydrogen bonded to the H90 residue (2.90A), the SO(2)NH(2) nitrogen atom forms a hydrogen bond with L352 (N O=2.80A), and the acetyl group is positioned in the vicinity of the S530 residue where the acetyl oxygen atom undergoes hydrogen bonding to L531 (2.99A). Nitrogen 236-244 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-126 21588529-2 2010 The Co(II) atom (site symmetry 2) is six-coordinate in a distorted octahedral configuration bonded by two N and two O atoms from two (2-amino-phen-yl)methanol ligands and two O atoms from the two nitrate anions. Nitrogen 106-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21522869-1 2011 In the title complex, [Co(NCS)(2)(C(13)H(19)N(3)O)(H(2)O)], the Co(II) ion is six-coordinated by the N,N",N""-tridentate Schiff base, the N atoms of two thio-cyanate ligands and one water mol-ecule in a distorted octa-hedral geometry. Nitrogen 26-27 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 21522869-1 2011 In the title complex, [Co(NCS)(2)(C(13)H(19)N(3)O)(H(2)O)], the Co(II) ion is six-coordinated by the N,N",N""-tridentate Schiff base, the N atoms of two thio-cyanate ligands and one water mol-ecule in a distorted octa-hedral geometry. Nitrogen 103-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 21522869-1 2011 In the title complex, [Co(NCS)(2)(C(13)H(19)N(3)O)(H(2)O)], the Co(II) ion is six-coordinated by the N,N",N""-tridentate Schiff base, the N atoms of two thio-cyanate ligands and one water mol-ecule in a distorted octa-hedral geometry. Nitrogen 44-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 21754318-1 2011 In the title compound, [Co(NO(3))(2)(C(18)H(16)N(2)O(2))], the Co(II) ion is six-coordinated in a distorted octa-hedral environment defined by two O and two N atoms from the ligand and by two O atoms from two nitrate anions. Nitrogen 27-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-69 21589279-2 2010 One Co(II) atom is coordinated by three O atoms from the three 2-hy-droxy-ethyl-pyridine (HEP) bridging ligands, two N atoms from two HEP ligands and one azido ligand, while the other Co(II) atom is coordinated by the same three O atoms, one N atom from an HEP ligand and two azido ligands. Nitrogen 117-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21589279-2 2010 One Co(II) atom is coordinated by three O atoms from the three 2-hy-droxy-ethyl-pyridine (HEP) bridging ligands, two N atoms from two HEP ligands and one azido ligand, while the other Co(II) atom is coordinated by the same three O atoms, one N atom from an HEP ligand and two azido ligands. Nitrogen 242-243 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 20708014-8 2010 Furthermore, inhibition of COX-2 activity by either NS-398 or DUP-697 partially offset protective effects of the miR-144/451 cluster. Nitrogen 52-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-32 20831162-5 2010 Based on the enthalpy, a weak N(2) interaction with the open Co(II) coordination sites is proposed for the first four phases, which is supported by Monte Carlo simulations. Nitrogen 30-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-66 21587471-2 2010 The Co(II) cation is in a distorted octa-hedral environment, coordinated by four sulfonate O atoms and two N atoms from the taurine ligands. Nitrogen 107-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21587689-2 2010 The Co(II) atom displays a distorted octa-hedral coordination geometry, provided by the O atoms of two monodentate ferrocene-carboxyl-ate anions and by the N and O atoms of two 2-pyridyl-methanol mol-ecule. Nitrogen 156-157 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 20405064-3 2010 Unusual selectivity for O(2) over N(2) (as high as 6.5) was demonstrated in the materials with open Co(ii) sites. Nitrogen 34-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 24061747-0 2010 Synthesis and Characterization of Co(II) Complexes of N-Thiophosphorylated Thioureas RC(S)NHP(S)(OiPr)2 (R = Me2N, 2-MeC6H4NH, 2,6-Me2C6H3NH, 2,4,6-Me3C6H2NH). Nitrogen 54-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-39 19860378-2 2009 Moreover, we have shown that the absence of a nitrogen atom in the spacer of the helicand ligand H(2)L(a), enables the assembly of an achiral mesohelical complex in the case of Co(II) ions. Nitrogen 46-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 177-183 20184343-1 2010 A highly effective Co(II)-based system has been developed for catalytic intramolecular C-H amination with phosphoryl azides without the need of terminal oxidant or other additives, resulting in the high-yielding production of cyclophosphoramidates with nitrogen gas as the byproduct. Nitrogen 253-261 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-24 19128155-5 2009 The two terminal Co(II) ions contain a facial coordination environment (3N, 3O) comprising three imino nitrogen atoms and three phenolate oxygen atoms. Nitrogen 103-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 19534677-4 2009 The derived QSAR models demonstrated that the COX-2 selectivity over COX-1 is predominantly influenced by the central core -N=C- of the diaryl system. Nitrogen 124-125 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-51 21582700-1 2009 In the title complex, [Co(C(22)H(24)N(2)O(4))] H(2)O, the Co(II) atom is in an almost square-planar coordination environment involv-ing two O and two N atoms from the Schiff base ligand. Nitrogen 36-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 58-64 21202733-2 2008 The Co(II) center is six-coordinated by four N atoms from one bis-[4-(2-pyrid-yl)pyrimidin-2-yl] sulfide (L) ligand and two bromide anions, forming an octa-hedral coordination geometry, where the four donor N atoms are located in the equatorial plane and the Br atoms occupy the axial positions. Nitrogen 45-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 19160097-9 2009 NS-398 dose-dependently decreased the levels of COX-2 mRNA, COX-2 protein, nuclear NF-kappaB protein and production of PGF(1alpha) and increased the cytoplasmic IkappaB protein. Nitrogen 0-2 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-53 19160097-9 2009 NS-398 dose-dependently decreased the levels of COX-2 mRNA, COX-2 protein, nuclear NF-kappaB protein and production of PGF(1alpha) and increased the cytoplasmic IkappaB protein. Nitrogen 0-2 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-65 21581217-1 2008 In the title compound, [Co(C(8)H(8)NO(3))(2)], the Co(II) atom lies on a centre of inversion and is coordinated in a slightly distorted square-planar geometry by two N and two O atoms from the 2-hydroxy-imino-methyl-6-methoxy-phenolate ligands. Nitrogen 35-36 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 21581110-1 2008 In the title complex, [Co(C(15)H(14)NO)(2)], the Co(II) atom, situated on an inversion centre, is coordinated by two O and two N atoms from two symmetry-related bidentate Schiff base ligands in a slightly distorted square-planar geometry. Nitrogen 36-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 18671849-11 2008 VEGF was significantly reduced following the treatment of NS-398 in A549 (by 31%) and MOR/P (by 47%) cells lines which expressing strong COX-2, but not in H460 cell line which expressing very low COX-2. Nitrogen 58-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-142 18671849-11 2008 VEGF was significantly reduced following the treatment of NS-398 in A549 (by 31%) and MOR/P (by 47%) cells lines which expressing strong COX-2, but not in H460 cell line which expressing very low COX-2. Nitrogen 58-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-201 21202733-2 2008 The Co(II) center is six-coordinated by four N atoms from one bis-[4-(2-pyrid-yl)pyrimidin-2-yl] sulfide (L) ligand and two bromide anions, forming an octa-hedral coordination geometry, where the four donor N atoms are located in the equatorial plane and the Br atoms occupy the axial positions. Nitrogen 207-208 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 15657055-5 2005 Single scattering fits of EXAFS data indicate that the metal ions in both native Zn(II)-containing and Co(II)-substituted VanX have the same coordination number and that the metal ions are coordinated by 5 nitrogen/oxygen ligands at approximately 2.0 angstroms. Nitrogen 206-214 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 18203712-1 2008 Cyclooxygenases (COX-1 and COX-2) are N-glycosylated, endoplasmic reticulum-resident, integral membrane proteins that catalyze the committed step in prostanoid synthesis. Nitrogen 38-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-32 16954617-1 2006 In the title compound, [CoCl2(C11H15N3O2)], the CoII ion is five-coordinated in a strongly distorted square-pyramidal arrangement, with one of the two Cl atoms located in the apical position, and the other Cl atom and the three N-donor atoms of the tridentate methyloxime ligand located in the basal plane. Nitrogen 36-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-52 15996511-4 2006 In the light of these results, it was suggested that two ligands coordinate to each metal atom by hydroxyl oxygen, imino nitrogen and thiazole ring nitrogen to form high spin octahedral complexes with Cr(III), Co(II), Ni(II) and Cu(II). Nitrogen 121-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 210-216 21202222-1 2008 In the mol-ecule of the title compound, [Co(C(6)H(4)NO(2))(2)(H(2)O)(2)], the coordination environment around the Co(II) atom is distorted octahedral; two N and two O atoms of the pyridine-2-carboxylate ligands lie in the equatorial plane and the two water O atoms in the axial positions. Nitrogen 52-53 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 17564434-1 2007 The properties of Cu(II) and Co(II) complexes with oxygen- or nitrogen-containing macrocycles have been extensively studied; however, less attention has been paid to the study of complexes containing sulfur atoms in the first coordination sphere. Nitrogen 62-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 16634581-13 2006 The coordination environment around the bridging Co(II) ion contains four oxygen (two P-O units, one chelating nitrate) and two nitrogen atoms (pyridyloxy nitrogens). Nitrogen 128-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 16634581-13 2006 The coordination environment around the bridging Co(II) ion contains four oxygen (two P-O units, one chelating nitrate) and two nitrogen atoms (pyridyloxy nitrogens). Nitrogen 155-164 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 15997066-3 2005 Each Co(II) ion is five-coordinated by two O and two N atoms from a Schiff base ligand, and by another bridging phenolate O atom from another Schiff base ligand, giving a severely distorted trigonal-bipyramidal coordination environment. Nitrogen 53-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 5-11 15875396-4 2004 The aim of this work is to study the retention mechanisms of Cu(II), Ni(II), and Co(II) on a BHA by means of a proper combination of physical and chemical techniques: sorption isotherms, mathematical modeling of these isotherms, molecular modeling, FTIR, and N2 (77 K) and CO2 (273 K) adsorption. Nitrogen 259-261 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 15289885-5 2004 The Cox-2 protein was strongly induced 2 h after exposure to n-LDL or Ox-LDL, the induction was maximal after 4 h and sustained for at least 8 h. The effect was specific for Cox-2, as Cox-1 expression was not modulated either by n-LDL or by Ox-LDL. Nitrogen 16-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-9 15289885-5 2004 The Cox-2 protein was strongly induced 2 h after exposure to n-LDL or Ox-LDL, the induction was maximal after 4 h and sustained for at least 8 h. The effect was specific for Cox-2, as Cox-1 expression was not modulated either by n-LDL or by Ox-LDL. Nitrogen 16-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 174-179 15289885-9 2004 The finding that n-LDL and Ox-LDL induces Cox-2 in human endothelial cells through a p38 MAPK, NF-kappaB, CREB dependent pathway thus modulating PGE2 release, suggests a new mechanism by which these lipoproteins induce endothelial dysfunction, sustaining inflammatory processes in the arterial wall. Nitrogen 6-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-47 14514319-3 2003 The temperature-dependent electronic and spectral properties of solutions containing the [Co(III)(tpy)(Cat-N-SQ)](+) suggest that this compound undergoes a thermally driven valence tautomeric interconversion to [Co(II)(tpy)(Cat-N-BQ)](+) complex, the metal ion being in high-spin configuration. Nitrogen 107-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-95 12971747-2 2003 Five nitrogen atoms complete the coordination sphere of the Co(II) ion, showing a distorted trigonal bipyramid geometry. Nitrogen 5-13 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 14520472-9 2003 This indicates that NF-kappaB activated by NS-398 is transcriptionally inactive and is an encouraging result for the use of COX-2-selective NSAIDs not only in chemoprevention but also as novel therapies for colon cancer. Nitrogen 43-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 124-129 12225948-8 2002 Hypoxia (3% O(2)-5% CO(2)-92% N(2)) for 24 h selectively augmented TGF-beta1-stimulated PGE(2) production and COX-2 induction but had no effect alone. Nitrogen 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-115 12536789-1 2002 CoII[N(CN)2]2(H2BiIm)2, 1, and [CoII[N(CN)2](H2BiIm)2]Cl, 2 (H2BiIm = 2,2"-biimidazole) have been structurally, spectroscopically, and magnetically characterized with both containing dicyanamides bound in unprecedented manners; namely, solely via the amide nitrogen for 1, and via an imide N forming 1-D helical chains for 2. Nitrogen 257-265 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-4 12517972-10 2003 Indo, NS-398, Flur, and 15d-PGJ(2), but not WY-14643, induced transcriptional activity of a COX-2 reporter construct containing the peroxisome proliferator response element (PPRE) on their own and enhanced the effect of IL-1beta, but had no effect on a COX-2 reporter construct lacking the PPRE. Nitrogen 6-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-97 12517972-10 2003 Indo, NS-398, Flur, and 15d-PGJ(2), but not WY-14643, induced transcriptional activity of a COX-2 reporter construct containing the peroxisome proliferator response element (PPRE) on their own and enhanced the effect of IL-1beta, but had no effect on a COX-2 reporter construct lacking the PPRE. Nitrogen 6-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 253-258 12007092-2 2002 Accurate single-crystal diffraction data were measured on a suitable crystal with Mo(K alpha) radiation at 125 K. The CoII ion is coordinated in a square bipyramidal fashion with four imino nitrogen atoms at the equatorial plane and two water molecules at the axial positions. Nitrogen 190-198 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-122 11842416-6 2002 With respect to the coordination sites, each Co(II) ion of the binuclear dioxygenated complexes is bound to one oxygen atom and four nitrogen atoms: N(pi) and N(tau) of two Carnos molecules, the peptide, and the terminal amino nitrogen atoms. Nitrogen 133-141 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 11935354-1 2002 The molecular modeling of Co(II)-bleomycin previously performed by us through NMR and molecular dynamics indicates that the most favorable structure for this complex is six-coordinate, with the secondary amine in beta-aminoalanine, the N5 and N1 nitrogens in the pyrimidine and imidazole rings, respectively, and the amide nitrogen in beta-hydroxyhistidine as equatorial ligands. Nitrogen 246-255 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 11935354-1 2002 The molecular modeling of Co(II)-bleomycin previously performed by us through NMR and molecular dynamics indicates that the most favorable structure for this complex is six-coordinate, with the secondary amine in beta-aminoalanine, the N5 and N1 nitrogens in the pyrimidine and imidazole rings, respectively, and the amide nitrogen in beta-hydroxyhistidine as equatorial ligands. Nitrogen 246-254 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 11935354-6 2002 The results of this investigation on Fe(II)- and Co(II)-bleomycin are most consistent with a six-coordinate structure with five endogenous N-donors and a solvent molecule or the carbamoyl group as the sixth ligand. Nitrogen 139-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 11842416-6 2002 With respect to the coordination sites, each Co(II) ion of the binuclear dioxygenated complexes is bound to one oxygen atom and four nitrogen atoms: N(pi) and N(tau) of two Carnos molecules, the peptide, and the terminal amino nitrogen atoms. Nitrogen 227-235 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 11377691-1 2001 The greater lability of Co(II) relative to Co(III) can potentially be used to achieve selective delivery of nitrogen mustard type molecules to hypoxic cells. Nitrogen 108-116 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 11487528-7 2001 Peroxynitrite, a highly reactive nitrogen molecule derived from the interaction of NO and superoxide anion, significantly increased COX-2 expression. Nitrogen 33-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-137 34464118-3 2021 Our experiments and density functional theory calculations indicate that the Co atom fixated into the nitrogen pots of g-C3N4 serves as the main active site, enabling dissociation of the adsorbed PAA and conversion of the coordinated Co(II) to Co(IV) via a unique two-electron transfer mechanism. Nitrogen 102-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 234-240 11457072-4 2001 Since EPR theory predicts an increase in Co(II) hyperfine splitting as donation from the axial N-donor ligand decreases, EPR spectroscopy could clarify the X-ray results. Nitrogen 95-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 11670380-4 1998 These organometallic Co(III) complexes underwent facile oxidative migration of the Co-bound vinyl group to a porphyrin pyrrole nitrogen when treated with Fe(III) salts or HClO(4) to provide moderate to good yields of Co(II) vinylene-N,N"-linked multi(porphyrin) complexes. Nitrogen 127-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 217-223 11670166-11 1997 The charge distribution in Tp(Cum,Me)Co(3,5-DBSQ) is Co(II)-SQ, rather than the more common Co(III)-Cat, due to surprisingly weak donation by the Tp(Cum,Me) nitrogens. Nitrogen 157-166 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-59 21639304-2 1997 Exhaustive adsorption of Ni(II) or Co(II) complexes, in the 0-4 mug L(-)(1) concentration range, was achieved by vibrationally promoted electrolysis for 3 min of ~25 muL volume samples, hanging under the working electrode in a nitrogen atmosphere. Nitrogen 227-235 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 9126611-5 1997 Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained. Nitrogen 36-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-48 9126611-6 1997 High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells. Nitrogen 15-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 9126611-8 1997 N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6. Nitrogen 4-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 8907587-6 1996 Five experimental compounds CGP-28238, Dup-697, NS-398, SC-58125 and L-745,337, have a greater selectivity for Cox-2. Nitrogen 48-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 111-116 34822668-6 2021 In this study, the production of proinflammatory mediators, such as nitrogen oxide and prostaglandin E2, was induced by 1-NP in a concentration-dependent manner through the expression of iNOS and COX2. Nitrogen 68-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-200 29712162-1 2001 mu4 end-on coordination (through the N atom) of the pseudohalogeno ligands X- =N3- and NCO- has been observed in the isostructural nonanuclear CoII cages with the general formula [Co9 {(2-C5 H4 N)2 CO2 }4 (O2 CMe)8 X2 ]; this mode is imposed by the trapping of anions X- into cavities formed inside the cage. Nitrogen 37-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-147 7832763-8 1995 Both NS-398 and Dup-697 exhibited time-dependent inactivation of hCOX-2, as did indomethacin on both enzymes. Nitrogen 5-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 65-71 35274660-2 2022 The magnetic anisotropy of sixteen seven-coordinate high-spin CoII complexes with O, N, Cl and I donors was investigated with state-of-the-art ab initio CASSCF/NEVPT2 calculations and compared with experimental data. Nitrogen 85-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-66 35442647-3 2022 These N vacancies enhanced the electron distribution of the Co 3d orbital and lowered the energy barrier to cleave the O-O bond of PMS in the Co(II)-PMS complex, achieving the modulation of major active species from 1O2 to Co(IV) O. Nitrogen 6-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-148 34292709-5 2021 Supported by an optimal chiral ligand, the Co(II)-based metalloradical system, which operates under mild conditions, is capable of 1,4-C-H alkylation of alpha-aryldiazoketones with varied electronic and steric properties to construct chiral alpha,beta-disubstituted cyclobutanones in good to high yields with high diastereoselectivities and enantioselectivities, generating dinitrogen as the only byproduct. Nitrogen 374-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-49 34611370-8 2021 The degradation of SMP in UV/Co(II)/PMS system was accomplished mainly by hydroxylation of the aromatic ring, extrusion of SO2, oxidation of NH2 group, and N - S bond cleavage. Nitrogen 156-157 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 35477280-1 2022 A new porous metal-organic framework, (Co (oba) (bpdh)) (DMF) (TMU-63), containing accessible nitrogen-rich diazahexadiene groups was successfully prepared with the solvothermal assembly of 5-bis(4-pyridyl)-3,4-diaza-2,4-hexadiene (4-bpdh), 4,4"-oxybis(benzoic) acid (oba), and Co(II) ions. Nitrogen 94-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 278-284 2827762-5 1987 Study of 6-coordinate O2-CoII(TPP)(L) complexes (L = nitrogenous base) using 14N- and 15N-labeled ligands and porphyrins enabled a detailed analysis of coupling parameters for both pyrrole and axial nitrogens. Nitrogen 199-208 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-29 35371547-4 2022 The CoII cations are coordinated by four N atoms of the cyclam ligand and two trans-S atoms of the tetra-thio-anti-monate anion within slightly distorted octa-hedra. Nitrogen 41-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 32717439-2 2020 Investigation of their molecular structure revealed that both complexes are isostructural and form analogous complex molecules, with a Co(II) atom hexacoordinated by two nitrogen atoms of bcp and four oxygen atoms of two chelate bonded flu (1) and nif (2) ligands in a distorted octahedral arrangement. Nitrogen 170-178 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 3722145-5 1986 It is also noted that the effect of the "extra" electron in the nitrogen base Co(II) oxy complexes, in some ways, parallels the effect of the lone pair electrons of thiolate in the oxy-P-450cam complex. Nitrogen 64-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 33533759-3 2021 In both the complexes, the CoII center has a distorted octahedral geometry with a CoN6 coordination environment, formed by four equatorial N atoms from the neutral ligand and two NCS- at the axial positions. Nitrogen 84-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-31 32846348-0 2020 Biostimulation of a marine anammox bacteria-dominated bioprocess by Co(II) to treat nitrogen-rich, saline wastewater. Nitrogen 84-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Nitrogen 24-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-77 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Nitrogen 24-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 208-212 32568423-3 2020 Atomic replacements of the Fe II by other metal(II) ions (e.g., Zn II /Co II ) via synthesizing isostructural trinuclear-complex precursors (Fe 2 Zn/Fe 2 Co), namely the "heteroatom modulator approach", realizes the inhibition of iron atoms aggregating toward nanoclusters with formation of a stable iron-dimer cluster in an optimal metal-nitrogen moiety within the carbon layer, clearly identified by direct transmission electron microscope imaging with X-ray absorption fine structure analyses. Nitrogen 339-347 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-76 32899627-2 2020 Almost all of the COX2 imaging agents using celecoxib as backbone were chemically modified in the position of N-atom in the sulfonamide group. Nitrogen 110-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-22 7309708-3 1981 The various spectral data indicated that the Co(II) center has tetrahedral geometry (high-spin state) and is linked by two nitrogens and two oxygens. Nitrogen 123-132 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 32846348-6 2020 The nitrogen removal with Co(II) addition could be well described by a modified Logistic model. Nitrogen 4-12 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 32022364-4 2020 Coordination of Co(II) ions into the porphyrin subunit followed by addition of appropriate monodentate nitrogen-based additives to function as axial ligands enable the radical carbene transfer reactions to styrene derivatives to occur exclusively through the cavity of the macrocycle to afford cyclopropane-linked rotaxanes in excellent 95% yield. Nitrogen 103-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-22 32456423-5 2020 Unlike (ArL)CoBr(N3(C6H4-p-tBu)), a series of alkyl azide-bound CoII analogues expel N2 only above 60 C, affording paramagnetic intermediates that convert to the corresponding Co-imine complexes via alpha-H-atom abstraction. Nitrogen 85-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-68 32008081-0 2020 Development of a liquid-nitrogen-induced homogeneous liquid-liquid microextraction of Co(II) and Ni(II) from water and fruit juice samples followed by atomic absorption spectrometry detection. Nitrogen 24-32 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-103 31691474-6 2020 The experimental studies and DFT calculations reveal that the high performance of the Co@FLG is mainly attributed to its great O2 absorptivity endowed by the abundant Co-Nx and pyridinic-N in the FLG shell and the strong electron-donating ability from the Co ND core to the FLG shell to elevate the eg-orbital energy of Co(II) and lower the activation energy for breaking the O=O/O-O bonds. Nitrogen 177-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 320-326 32008081-1 2020 In this study, a simple and rapid sample preparation method named liquid-nitrogen-induced homogeneous liquid-liquid microextraction has been developed for the extraction and pre-concentration of Co(II) and Ni(II) ions before their analysis by flame atomic absorption spectrometry. Nitrogen 73-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 195-201 31838698-7 2020 The relatively large surface area as estimated from N2 adsorption makes the nanopowders very favorable for the uptake Cd(II), Cr (IV), Co (II) and Ni(II) from aqueous solution. Nitrogen 52-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-153 31270632-12 2019 Graphical abstract Schematic presentation of the quenching of the fluorescence of phosphorus and nitrogen dually-doped carbon quantum dots (PN-CQDs) by vitamin B12 (VB12) and Co(II). Nitrogen 97-105 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-181 31380790-0 2019 Two CoII coordination polymers of biphenyl-2,2",5,5"-tetracarboxylic acid with flexible N-donor ligands: syntheses, structures and magnetic properties. Nitrogen 88-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 30884075-4 2019 When the resulting CoII -H species was exposed to N2 , H2 evolution readily occurs at ambient conditions. Nitrogen 50-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-23 30966264-0 2018 Two New Three-Dimensional Pillared-Layer Co(II) and Cu(II) Frameworks Involving a [M2(EO-N3)2] Motif from a Semi-Flexible N-Donor Ligand, 5,5"-Bipyrimidin: Syntheses, Structures and Magnetic Properties. Nitrogen 4-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 30951298-5 2019 The central transition-metal ion M n+ (MnII, FeIII, CoII, NiII, CuII, ZnII, PdII) in the POP structure and also the nature of the capping group (AsO43-, SeO32-, PO43-, phenyl-AsO32-) influence the resulting catalytic performance. Nitrogen 35-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-56 30724472-2 2019 Herein, we report on a unique strategy to prepare Fe-Co-N-C-x (x refers to the pyrolysis temperature) electrocatalysts which involves anion-exchange of [Fe(CN)6 ]3- into a cationic CoII -based metal-organic framework precursor prior to heat treatment. Nitrogen 56-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 181-185 30724472-4 2019 This is the first example of Fe-Co-N-C electrocatalysts fabricated from a cationic CoII -based MOF precursor that dopes the Fe element via anion-exchange, and our current work provides a new entrance towards MOF-derived transition-metal (e.g. Fe or Co) and nitrogen-codoped carbon electrocatalysts with excellent ORR activity. Nitrogen 257-265 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-87 30585716-4 2019 Removing just one nitrogen linker between the Co(II)-binding bipyridine groups has a profound impact on the molecular geometry observed by single crystal analysis. Nitrogen 18-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 30960859-9 2018 In the series of Co(II)/AlEt2Cl binary systems, complexes containing electron-withdrawing N-aryl substituents (R = 4-CF3, 2,6-2F) afforded higher molecular weights polyisoprene than that was obtained by the complex containing electron-donating N-alkyl substituents (R = octyl). Nitrogen 90-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 30310585-3 2018 Herein, we report the synthesis of a novel redox active ligand, [ibaps]3-, which binds to transition metals such as FeII and CoII in a meridional fashion through the three anionic nitrogen atoms and provides additional coordination sites for other ligands. Nitrogen 180-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-129 29400411-10 2018 They linked to COX-2 through the N atom of the azole scaffold, while C O of the oxazolone moiety was responsible for the binding to amino acids inside the LOX active site. Nitrogen 33-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-20 28118518-4 2017 The alteration of the D value by N-bound axial CN ligands, upon association with cyanometallates, was also assessed for heptacoordinated FeII as well as for related NiII and CoII derivatives. Nitrogen 33-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 174-178 29250408-2 2017 Each CoII ion is coordinated by two pyridine N atoms from two bridging L ligands, two O atoms from methanol mol-ecules and two chloride anions, all inversion-related. Nitrogen 45-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 5-9 29152374-2 2017 The CoII cations are coordinated by two terminal N-bonding thio-cyanate anions and four N-bonding pyridine-4-carbo-thio-amide ligands, resulting in discrete and slightly distorted octa-hedral complexes. Nitrogen 49-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 29152374-2 2017 The CoII cations are coordinated by two terminal N-bonding thio-cyanate anions and four N-bonding pyridine-4-carbo-thio-amide ligands, resulting in discrete and slightly distorted octa-hedral complexes. Nitrogen 88-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 28846901-1 2018 A novel nitrogen-doped biochar embedded with cobalt (Co-NB) was fabricated via pyrolysis of glucose pretreated with melamine (N donor) and Co(II). Nitrogen 8-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-145 29231218-1 2018 We successfully developed an approach to synthesize a metal oxide- and N-codoped carbon nanosheet, NC@CoO/CuO, derived from a metal-organic framework nanofiber, Cu(ii)-Asp@Co(II) (Asp = l-aspartate). Nitrogen 71-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 172-178 28525865-3 2017 This bidentate ligand coordinates three metal ions of Co(II), Cu(II) and Fe(II) via nitrogen and oxygen atoms. Nitrogen 84-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 25105264-3 2015 The infrared spectra of Co(II), Ni(II) and Cu(II) complexes indicate a bidentate type of bonding for APC through the exocyclic amino and adjacent pyrimidine nitrogen as donors whereas APC coordinated to Pd(II) ion as a monodentated ligand via a pyrimidine nitrogen donor. Nitrogen 157-165 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 27367692-2 2016 Based on a selectivity study, the SG-APTMS-N,N-EPANTf2 phase showed a perfect selectivity towards Zr(IV) at pH 4 as compared to other metallic ions, including gold [Au(III)], copper [Cu(II)], cobalt [Co(II)], chromium [Cr(III)], lead [Pb(II)], selenium [Se(IV)] and mercury [Hg(II)] ions. Nitrogen 43-44 mitochondrially encoded cytochrome c oxidase II Homo sapiens 200-207 26213094-0 2015 Biphenyl-2,4,6,3",5"-pentacarboxylic acid as a tecton for six new Co(II) coordination polymers: pH and N-donor ligand-dependent assemblies, structure diversities and magnetic properties. Nitrogen 103-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 25218230-1 2015 New Co(II), Ni(II) and Cu(II) complexes derived from tetradentate macrocyclic nitrogen ligand, (1E,4E,8E,12E)-5,8,13,16-tetramethyl-1,4,9,12-tetrazacyclohexadeca-4,8,12,16-tetraene (EDHDH) have been synthesized. Nitrogen 78-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 27746942-2 2016 The CoII ion is coordinated in a slightly distorted trigonal-bipyramidal environment which is defined by three O atoms occupying the equatorial plane and the N and Cl atoms in the apical sites. Nitrogen 158-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 26594532-2 2015 The Co(II) ion has a slightly distorted octahedral coordination environment which is defined by two N atoms occupying the apical position, while the equatorial plane is furnished by two hy-droxy O atoms and two carboxyl-ate O atoms. Nitrogen 100-101 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 26139944-3 2015 In addition to generating the environmentally benign N2 as the only byproduct, this Co(II)-based metalloradical aziridination process features mild reaction conditions and operational simplicity. Nitrogen 53-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-89 25469667-2 2015 CoCr surfaces modified by nitrogen plasma immersion ion implantation (PIII) are characterized by improved wear resistance but also showed increased Co(II) ion release under in vitro conditions. Nitrogen 26-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 148-153 25548276-10 2015 We conclude that N-glycosylation of Asn-594 of COX-2 occurs in the ER, leading to anterograde movement of COX-2 to the Golgi where the Asn-594-linked glycan is trimmed prior to retrograde COX-2 transport to the ER for ERAD. Nitrogen 17-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-52 25548276-10 2015 We conclude that N-glycosylation of Asn-594 of COX-2 occurs in the ER, leading to anterograde movement of COX-2 to the Golgi where the Asn-594-linked glycan is trimmed prior to retrograde COX-2 transport to the ER for ERAD. Nitrogen 17-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-111 25548276-10 2015 We conclude that N-glycosylation of Asn-594 of COX-2 occurs in the ER, leading to anterograde movement of COX-2 to the Golgi where the Asn-594-linked glycan is trimmed prior to retrograde COX-2 transport to the ER for ERAD. Nitrogen 17-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-111 25105264-3 2015 The infrared spectra of Co(II), Ni(II) and Cu(II) complexes indicate a bidentate type of bonding for APC through the exocyclic amino and adjacent pyrimidine nitrogen as donors whereas APC coordinated to Pd(II) ion as a monodentated ligand via a pyrimidine nitrogen donor. Nitrogen 256-264 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 24888451-1 2014 Reaction of Co(II) with the nitrogen-rich ligand N,N-bis(1H-tetrazole-5-yl)-amine (H2bta) leads to a mixed-valence, 3D, porous, metal-organic framework (MOF)-based, energetic material with the nitrogen content of 51.78%, [Co9(bta)10(Hbta)2(H2O)10]n (22 H2O)n (1). Nitrogen 28-36 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 24888451-1 2014 Reaction of Co(II) with the nitrogen-rich ligand N,N-bis(1H-tetrazole-5-yl)-amine (H2bta) leads to a mixed-valence, 3D, porous, metal-organic framework (MOF)-based, energetic material with the nitrogen content of 51.78%, [Co9(bta)10(Hbta)2(H2O)10]n (22 H2O)n (1). Nitrogen 193-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18