PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12465804-4 2003 Also, for the first time a plausible correlation between the released Mg(II) ions from sepiolite matrix and those adsorbed Co(II) ions is made. mg(ii) 70-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-129 15214085-4 2004 Whereas the paramagnetic metal cations Cu(II), Fe(II), Ni(II), Co(II), and Mn(II) result in fluorescence quenching, the emission response is not altered by millimolar concentrations of Ca(II) or Mg(II), rendering the sensors selective for Zn(II) among all biologically important metal cations. mg(ii) 195-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-68 11106490-9 2000 The only other metal ion to cause slight activation of the enzyme was Co(II), with Ca(II), Cu(II), Mg(II), Ni(II), and Zn(II) all being inhibitory. mg(ii) 99-105 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-76 12203329-10 2002 The Zn(II) and Mg(II) complexes were all far less stable than the corresponding Ni(II) and Co(II) complexes. mg(ii) 15-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 9328176-9 1997 Interestingly, in the absence of Mg(II), the activity of the enzymes could be restored by Co(II) to 73% of that with Mg(II) alone for MutT, and 34% for MTH1, the other metals being much less or non-effective. mg(ii) 117-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-96 117692-1 1978 In the present study use was made of the chelating ability of EDTA and the activating property of some metal ions Ca(II), Mg(II) or Mn(II) to counteract the inhibitory effect of Cu(II), Co(II), Pb(II) or Zn(II) ions on the B6-dependent kynurenine hydrolase and on kynurenine aminotransferase. mg(ii) 122-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 186-192 30667210-9 2019 Density functional theory calculations elucidate the discrepancy in CO affinity: Co(II) and Ni(II) form strong pi-back-donating bonds with CO via electron transfer from the d orbitals of the transition metals to the antibonding molecular orbitals of CO, whereas Mg(II) does not participate in electron transfer or orbital overlap with CO. mg(ii) 262-268 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87