PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29355485-0 2018 COX16 is required for assembly of cytochrome c oxidase in human cells and is involved in copper delivery to COX2. Copper 89-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-112 29355485-10 2018 Finally, we found that copper supplementation increases COX activity and restores normal steady state levels of COX subunits in COX16 knockout cells, indicating that, even in the absence of a canonical copper binding motif, COX16 could be involved in copper delivery to COX2. Copper 23-29 mitochondrially encoded cytochrome c oxidase II Homo sapiens 270-274 26160915-7 2015 Our data reveal that COA6 is intricately involved in the copper-dependent biogenesis of COX2. Copper 57-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-92 29381136-2 2018 The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. Copper 78-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-50 26160915-4 2015 Complete loss of COA6 activity using gene editing in HEK293T cells resulted in a profound growth defect due to complex IV deficiency, caused by impaired biogenesis of the copper-bound mitochondrial DNA-encoded subunit COX2 and subsequent accumulation of complex IV assembly intermediates. Copper 171-177 mitochondrially encoded cytochrome c oxidase II Homo sapiens 218-222 29154948-2 2018 Upon synthesis, COX2 engages with COX20 in the inner mitochondrial membrane, a scaffold protein that recruits metallochaperones for copper delivery to the CuA-Site of COX2. Copper 132-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-20 29154948-2 2018 Upon synthesis, COX2 engages with COX20 in the inner mitochondrial membrane, a scaffold protein that recruits metallochaperones for copper delivery to the CuA-Site of COX2. Copper 132-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-38 26859480-2 2016 Although Cu(i/ii), Co(ii), Ag(i), and Zn(ii) coordination to thione and selone ligands has been broadly studied and Fe(ii) plays an important role in oxidative damage, very few iron-thione complexes and no iron-selone complexes are reported. Copper 9-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-16 26669719-4 2016 Here we show that yeast Coa6 is an orthologue of human COA6, and like Cox2, is regulated by copper availability, further implicating it in copper delivery to Cox2. Copper 92-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 26669719-4 2016 Here we show that yeast Coa6 is an orthologue of human COA6, and like Cox2, is regulated by copper availability, further implicating it in copper delivery to Cox2. Copper 92-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 158-162 26669719-4 2016 Here we show that yeast Coa6 is an orthologue of human COA6, and like Cox2, is regulated by copper availability, further implicating it in copper delivery to Cox2. Copper 139-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 26669719-4 2016 Here we show that yeast Coa6 is an orthologue of human COA6, and like Cox2, is regulated by copper availability, further implicating it in copper delivery to Cox2. Copper 139-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 158-162 25959673-2 2015 COX1 and COX2 contain heme and copper redox centers, which are integrated during assembly of the enzyme. Copper 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-13 25959673-6 2015 COA6 interacts transiently with the copper-containing catalytic domain of newly synthesized COX2. Copper 36-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-96 25959673-9 2015 Our analyses define COA6 as a constituent of the mitochondrial copper relay system, linking defects in COX2 metallation to cardiac cytochrome c oxidase deficiency. Copper 63-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-107 20657935-1 2010 The systematic immobilization of cobalt(II) Schiff base complexes on SBA-15 mesoporous silica via copper catalyzed [3 + 2] azide-alkyne cycloaddition (CuAAC) "click reaction" involving either step-wise synthesis of silica-bound Schiff base ligand followed by its subsequent complexation with cobalt ions, or by the direct immobilization of preformed Co(II) Schiff base complex to the silica support is described. Copper 98-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 350-355 22803970-7 2012 The crystal structures of Cu(I) and Ag(I) complexes revealed the dinuclear nature with characteristic metallophilic interactions [M M] (M = Cu, Ag), while the Cu(II) and Co(II) complexes were mononuclear. Copper 26-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 172-178 21796325-4 2011 The interaction of Co(II), Ni(II) and Cu(II) with the unsymmetric macrocycle series has been investigated by potentiometric (pH) titration in 95% methanol; X-ray structures of two nickel and three copper complexes of these ligands, each exhibiting 1:1 (M:L) ratios, have been obtained. Copper 197-203 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 21214033-6 2010 At the optimum conditions, the copper extraction was approximately 90%, significantly greater than that of the other coexisting ions--nickel(II) [Ni(II)], cobalt(II) [Co(II)], and manganese(II) [Mn(II)]. Copper 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 167-173 19393246-7 2009 This observation may indicate that the absence of Cox17 interferes with copper delivery to Cox2, but not to Cox1. Copper 72-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-95 20455576-2 2010 The addition of Cu to reactions with Co(II), Fe(III), or Mn(II) leads to the formation of heterobimetallic UMCM-150 isostructural analogues Co(1)Cu(2)(BHTC)(2) (4), Fe(1)Cu(2)(BHTC)(2) (5), and Mn(1)Cu(2)(BHTC)(2) (6) containing both paddlewheel and trinuclear metal clusters. Copper 16-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-43 20455576-2 2010 The addition of Cu to reactions with Co(II), Fe(III), or Mn(II) leads to the formation of heterobimetallic UMCM-150 isostructural analogues Co(1)Cu(2)(BHTC)(2) (4), Fe(1)Cu(2)(BHTC)(2) (5), and Mn(1)Cu(2)(BHTC)(2) (6) containing both paddlewheel and trinuclear metal clusters. Copper 145-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-43 19954165-11 2010 Under similar conditions, the 3-Hfl complexes of Co(II), Ni(II), and Cu(II) undergo flavonolate ligand exchange to produce [(6-Ph(2)TPA)M(CD(3)CN)(n)](X)(2) (M = Co, Ni, Cu; n = 1 or 2) and [Zn(3-Hfl)(2).2H(2)O]. Copper 69-71 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 19399766-3 2009 The large selectivity is ascribed to the redox-active nature of copper which enables a reduction from Cu(II) to Cu(I), occurring upon ESI-MS, whereas Co(II), Ni(II) and Zn(II) cannot undergo similar redox reactions. Copper 64-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-156 19336478-7 2009 The subsequent maturation of CO II is contingent upon the formation of a complex that includes both SCO proteins, each with a functional CxxxC copper-coordinating motif. Copper 143-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-34 19295170-1 2009 Sco1 and Sco2 are mitochondrial copper-binding proteins involved in the biogenesis of the Cu(A) site in the cytochrome c oxidase (CcO) subunit Cox2 and in the maintenance of cellular copper homeostasis. Copper 32-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-147 19295170-1 2009 Sco1 and Sco2 are mitochondrial copper-binding proteins involved in the biogenesis of the Cu(A) site in the cytochrome c oxidase (CcO) subunit Cox2 and in the maintenance of cellular copper homeostasis. Copper 183-189 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-147 18390903-1 2008 Sco1 is implicated in the copper metallation of the Cu(A) site in Cox2 of cytochrome oxidase. Copper 26-32 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-70 18473059-1 2008 Discrete homo Cu-Cu-Cu and hetero Cu-Pd-Cu or Cu-Co-Cu metal arrays are prepared within an organic-pillared coordination box by inserting M(ii)-azaporphine/porphine cartridges (M = Cu(ii), Pd(ii) or Co(ii)), where the metal arrays show unique spin interactions in ESR: in particular, Deltam(s) = 3 for the Cu-Cu-Cu array. Copper 14-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-142 17029361-1 2006 The coordination of the cations Cu(II), Co(II), Rh(III), Ir(III), Ni(II), Pd(II), Pt(II), and Zn(II) to the copper-binding octapeptide region in the human prion protein has been compared through structural optimization. Copper 108-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 17386604-5 2007 The selectivity coefficients (S(Cu/Me)) for Me=Ni(II), Co(II) are 45.0 and 38.5, respectively. Copper 32-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 16023340-7 2006 However, Co(II)-uptake was inhibited in presence of other metals (Pb, Cd, Cu, Ni, Cr and Zn). Copper 74-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-14 15627369-4 2005 on the other hand, for Mn(ii) and Fe(ii) ions, L(Cu) shows a 2-carboxylate bridging mode to form an another 1-d assembly with a repeating motif of [-M-O-C-O-CU-O-C-O-]: [ML(Cu)(H(2)O)(4)](N)() (M = Mn (7), Fe (8)). Copper 49-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-28 16083427-3 2005 SCO2 is a copper-binding protein presumably involved in formation of the Cu(A) centre of the COX2 subunit. Copper 10-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-97 15674245-5 2005 Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. Copper 43-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-172 15674245-5 2005 Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. Copper 64-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-172 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Copper 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 254-256 15627369-4 2005 on the other hand, for Mn(ii) and Fe(ii) ions, L(Cu) shows a 2-carboxylate bridging mode to form an another 1-d assembly with a repeating motif of [-M-O-C-O-CU-O-C-O-]: [ML(Cu)(H(2)O)(4)](N)() (M = Mn (7), Fe (8)). Copper 49-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-39 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Copper 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Copper 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 267-273 15627369-4 2005 on the other hand, for Mn(ii) and Fe(ii) ions, L(Cu) shows a 2-carboxylate bridging mode to form an another 1-d assembly with a repeating motif of [-M-O-C-O-CU-O-C-O-]: [ML(Cu)(H(2)O)(4)](N)() (M = Mn (7), Fe (8)). Copper 157-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-28 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Copper 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Copper 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15627369-4 2005 on the other hand, for Mn(ii) and Fe(ii) ions, L(Cu) shows a 2-carboxylate bridging mode to form an another 1-d assembly with a repeating motif of [-M-O-C-O-CU-O-C-O-]: [ML(Cu)(H(2)O)(4)](N)() (M = Mn (7), Fe (8)). Copper 157-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-39 11721898-4 2001 The CL intensity decreased in the order mono- > di- > triethanolamine and Co(II) > Cu(II) > Ni(II) > Fe-(III) > Mn(II) > Fe(II). Copper 92-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-86 12759799-7 2003 Application of the method to the speciation of Co(II), Co(III), and Cu(II) in copper-plating bath samples is also demonstrated. Copper 78-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 18969136-3 2003 The extraction of copper is affected by Fe(II), Mn(II), Zn(II), Ni(II) and Co(II) while only Fe(II) interferes in the lead determination. Copper 18-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 75-81 10954195-3 2000 Sco1/2 proteins have been isolated as high-copy number suppressors of a deletion of copper chaperone Cox 17, implicating Sco1/2 in copper transport to COX subunits I or II. Copper 84-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-171 10954195-3 2000 Sco1/2 proteins have been isolated as high-copy number suppressors of a deletion of copper chaperone Cox 17, implicating Sco1/2 in copper transport to COX subunits I or II. Copper 131-137 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-171 18967436-4 1998 The method proposed was applied in the analysis of a new type electroless copper plating solutions containing Co(II)-ethylenediamine complex compounds as reducing agents. Copper 74-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-116 35210360-5 2022 COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2. Copper 36-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-187 35210360-5 2022 COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2. Copper 167-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-187 3411318-2 1988 This effect was detected on the enzyme having Co(II) substituted for the native Zn(II), in which the resonances of residues bound to the copper are detected because of the antiferromagnetic coupling between Cu(II) and Co(II). Copper 137-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 35053273-2 2022 Copper is bound to COX1 and COX2, two core subunits of CcO, forming the CuB and CuA sites, respectively. Copper 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-32 35053273-6 2022 Initial genetic and biochemical studies have linked COA6 with copper delivery to COX2 and follow-up structural and functional studies have shown that it is specifically required for the biogenesis of the CuA site by acting as a disulfide reductase of SCO and COX2 proteins. Copper 62-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-85 2484613-5 1989 Cu(I), Cu(II), Co(II), and Ni(II) induced a predominant generation of FdU, with copper ions being more effective than Co and Ni. Copper 80-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-20 3411318-2 1988 This effect was detected on the enzyme having Co(II) substituted for the native Zn(II), in which the resonances of residues bound to the copper are detected because of the antiferromagnetic coupling between Cu(II) and Co(II). Copper 137-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 218-224 6322852-0 1984 Co(II) derivatives of Cu,Zn-superoxide dismutase with the cobalt bound in the place of copper. Copper 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 3335495-2 1988 The Cu,Co superoxide dismutase derivative, in which the native Zn(II) was replaced by Co(II), was investigated by 1H NMR spectroscopy at pH 7.0 in the presence of CN- and N-3. Copper 4-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 6322852-2 1984 Co(II) derivatives of Cu,Zn-superoxide dismutase having cobalt substituted for the copper (Co,Zn-superoxide dismutase and Co,Co-superoxide dismutase) were studied by optical and EPR spectroscopy. Copper 83-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 6322852-13 1984 These results substantiate the contention that Co(II) can replace the copper of Cu,Zn-superoxide dismutase in a way that reproduces the properties of the native copper-binding site. Copper 70-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 6322852-13 1984 These results substantiate the contention that Co(II) can replace the copper of Cu,Zn-superoxide dismutase in a way that reproduces the properties of the native copper-binding site. Copper 161-167 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 6794641-0 1981 X-ray absorption edge spectroscopy of Co(II)-binding sites of copper- and zinc-containing proteins. Copper 62-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 6280674-10 1981 By adding Co2+ ions to the vacant copper site of [Cu1--Zn2] a hybrid molecule containing Cu(II) on one subunit and Co(II) in the homologous site of the other subunit was prepared. Copper 34-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 115-121 6794641-2 1981 Significant differences, detected in the spectrum of the [Cu(II)-Co(II)] derivative as compared to the other species, indicate that a conformational change and/or a different charge of the imidazole bridging the two metal sites in superoxide dismutase occur in coincidence with the change of copper valence. Copper 292-298 mitochondrially encoded cytochrome c oxidase II Homo sapiens 65-71 32271545-5 2020 The possible interface mechanism of PMS activation by CuCo-H3 was proposed, wherein unique interconnected meso-macroporous nanosheets structure, strong interaction between copper and cobalt, and cycling of Co(II)/Co(III) and Cu(I)/Cu(II) effectively facilitated PMS activation to generate SO4 - and OH, which contributed to BP-4 degradation. Copper 172-178 mitochondrially encoded cytochrome c oxidase II Homo sapiens 206-212 163245-1 1975 High resolution electron spin resonance spectra of the stepwise formation of CN- complexes of Co(II) and Cu(II) carbonic anhydrase show that both metal enzymes form successive 1:1 and 2:1 addition products with CN- at 112 K. The 1:1 complex with the Cu(II) enzyme has a rhombic ESR spectrum similar to the spectra of the 1:1 complexes of the Cu(II) enzyme with CH3COO-, OCN-, N3-, and SH-. Copper 105-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 33497983-6 2021 Quenching reactions and EPR studies revealed the coexistence of sulfate radical (SO4 -), hydroxyl radical ( OH), and singlet oxygen (1O2), which was attributed to the potential in-situ recycling of cobalt and copper species (Co(III) Co(II), Cu(II) Cu(I))). Copper 209-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 233-239 33169484-5 2021 We hypothesize that COX16 could play a role in the copper delivery route of the COX2 module as part of the complex IV assembly. Copper 51-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-84 32229208-5 2020 In addition, the significance of inserting the Cu(II) ions recognition cavities within the adsorbent matrix was pointed out by performing the adsorption in a multi-ionic solution mixture containing Co(II), Ni(II), Pb(II), Cd(II) and Cu(II) ions and the obtained selectivity coefficients in case of Cu-CIS revealed remarkable selectivity potentials toward the Cu(II) ions compared to NI-CIS. Copper 47-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 198-204 31910337-4 2020 In particular, Mn(II), Co(II), Ni(II), and Cu(II) were reported for the first time to form such large and discrete structures with (tpy-M-tpy) connectivity. Copper 43-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-29 31832781-1 2020 In this work, mixed ligand complexes of Co(II) Ni(II) and Cu(II) were synthesized using quercetin and diimine (1,10-phenanthroline or 2,2"-bipyiridine) ligands. Copper 58-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 31832781-2 2020 The obtained Ni(II) and Co(II) complexes are new and the Cu(II) complexes are synthesized by different method from the literature. Copper 57-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 32061935-2 2020 The conserved COX2 subunit contains the CuA site, a binuclear copper center. Copper 40-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-18 32061935-2 2020 The conserved COX2 subunit contains the CuA site, a binuclear copper center. Copper 62-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-18 31935603-6 2020 Co(II) complex (1) exhibited enhanced catecholase activity with Kcat = 213.48 h-1, which is attributed to the greater extent of charge contribution on Co2+ as compared to Cu2+ as determined by DFT calculations. Copper 171-175 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 31851937-2 2019 Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6, a recently discovered protein whose molecular function is unknown. Copper 13-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 31851937-3 2019 To uncover the molecular mechanism by which COA6 and SCO proteins mediate copper delivery to COX2, we have solved the solution structure of COA6, which reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. Copper 74-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-97 31851937-4 2019 Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Copper 136-142 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-121 31851937-4 2019 Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Copper 53-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-121 31903891-2 2019 Cox17 shuttles copper ions from the cytosol to the mitochondria and, together with Sco1 and Sco2, provides copper ions to the Cox1 and Cox2 mitochondrially encoded subunits. Copper 15-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-139 30580142-4 2019 Capturing cobalt (Co(II)) from filtered river water doped with competing metals (Cu, As, Ag, Cd, Hg, Tl, and Pb) was most effective from pH 5-8 with binding affinity ranged from IDAA > DE4A > ED3A > Ac-Phos > SH on SAMMS. Copper 81-83 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 30918270-10 2019 Additionally, we also predicted the mechanism of action of the copper complexes 1-3 using molecular modeling studies with COX-2 inhibitor. Copper 63-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-127 31903891-2 2019 Cox17 shuttles copper ions from the cytosol to the mitochondria and, together with Sco1 and Sco2, provides copper ions to the Cox1 and Cox2 mitochondrially encoded subunits. Copper 107-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-139 29702455-8 2018 XPS analysis confirmed that substitution of copper could promote the cycle of CoII/CoIII, thus enhance the catalytic efficiency for PMS activation. Copper 44-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-82 29492773-5 2018 The ability of these metal ions to produce oligosaccharide adduct ions by ESI had the general trend: Ca(II) > Mg(II) > Ni(II) > Co(II) > Zn(II) > Cu(II) > Na(I) > K(I) > Al(III) Fe(III) Cr(III). Copper 161-163 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143