LEADER 01244nam 2200349Ia 450 001 996397103803316 005 20221108071205.0 035 $a(CKB)4940000000059175 035 $a(EEBO)2240896796 035 $a(OCoLC)13656779 035 $a(EXLCZ)994940000000059175 100 $a19860529d1645 uy | 101 0 $aeng 135 $aurbn||||a|bb| 200 12$aA divine discovery of sincerity according to its proper and peculiar nature$b[electronic resource] $every profitable for all sorts of persons to peruse : first preached and now published for the good of Gods church in generall /$fby Nicholas Lockyer .. 210 $aLondon $cPrinted by Edward Griffin for Iohn Rothwell ...$d1645 215 $a[12], 148 p 300 $aReproduction of original in Huntington Library. 330 $aeebo-0113 606 $aSincerity$vSermons 606 $aSincerity$vEarly works to 1800 615 0$aSincerity 615 0$aSincerity 700 $aLockyer$b Nicholas$f1611-1685.$01001384 801 0$bEAA 801 1$bEAA 801 2$bm/c 801 2$bWaOLN 906 $aBOOK 912 $a996397103803316 996 $aA divine discovery of sincerity according to its proper and peculiar nature$92394449 997 $aUNISA LEADER 03090nam 2200577 450 001 9910797445503321 005 20200923020339.0 010 $a3-11-043658-2 024 7 $a10.1515/9783110436587 035 $a(CKB)3710000000455826 035 $a(DE-B1597)456526 035 $a(OCoLC)979746048 035 $a(DE-B1597)9783110436587 035 $a(MiAaPQ)EBC5024742 035 $a(Au-PeEL)EBL5024742 035 $a(CaPaEBR)ebr11567603 035 $a(EXLCZ)993710000000455826 100 $a20110504d2009 uy| 0 101 0 $aeng 135 $aur||||||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aMetal-carbon bonds in enzymes and cofactors /$fedited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel 210 1$aCambridge, UK :$cRSC Publishing,$d2009. 215 $a1 online resource 225 1 $aMetal ions in life sciences,$x1559-0836 ;$vvolume 6 311 $a3-11-044279-5 320 $aIncludes bibliographical references and indexes. 327 $aOrganometallic chemistry of B12 coenzymes -- Cobalamin- and corrinoid-dependent enzymes -- Nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase -- Nickel-carbon bonds in acetyl-coenzyme a synthases/carbon monoxide dehydrogenases -- Structure and function of [NiFe]-hydro-genases -- Carbon monoxide and cyanide ligands in the active site of [FeFe]-hydrogenases -- Carbon monoxide as intrinsic ligand to iron in the active site of [Fe]-hydrogenase -- Dual role of heme as cofactor and substrate in the biosynthesis of carbon monoxide -- Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site -- Interaction of cyanide with enzymes containing vanadium, manganese, non-heme iron, and zinc -- Reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds. 330 $aThe occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, is only recently recognized. Of course, the historical examples are the B12 coenzymes containing cobalt-carbon bonds, but now such bonds are also known for nickel, iron, copper, and other transition metal ions. There is no other comparable book; MILS-6, written by 17 experts, summarizes the most recent insights into this fascinating topic. 410 0$aMetal ions in life sciences ;$vv. 6. 606 $aMetalloenzymes 606 $aCoenzymes 606 $aOrganometallic compounds 606 $aVitamin B12 615 0$aMetalloenzymes. 615 0$aCoenzymes. 615 0$aOrganometallic compounds. 615 0$aVitamin B12. 676 $a572.7 702 $aSigel$b Astrid 702 $aSigel$b Helmut 702 $aSigel$b Roland K. 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