| Record ID | ia:metalsitesinprot0000unse_o0d4 |
| Source | Internet Archive |
| Download MARC XML | https://archive.org/download/metalsitesinprot0000unse_o0d4/metalsitesinprot0000unse_o0d4_marc.xml |
| Download MARC binary | https://www.archive.org/download/metalsitesinprot0000unse_o0d4/metalsitesinprot0000unse_o0d4_meta.mrc |
LEADER: 03956cam 2200961 a 4500
001 ocm37798433
003 OCoLC
005 20181218195901.0
008 971017s1997 gw a b 001 0 eng d
010 $a 97208969
040 $aABAU$beng$cDLC$dNLM$dABC$dAGL$dOHX$dBAKER$dNLGGC$dYDXCP$dBTCTA$dOCLCG$dZWZ$dGEBAY$dSCB$dIAD$dOCLCF$dDEBSZ$dOCLCQ$dUKMGB
016 7 $a9717711$2DNLM
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019 $a1045189296
020 $a3540628703
020 $a9783540628705
035 $a(OCoLC)37798433$z(OCoLC)1045189296
042 $alccopycat
050 04 $aQD461$b.S92 vol. 88$aQP601.7
060 00 $aW1$bST82K v.88 1997
060 10 $aQU 125$bM587 1997
070 0 $aQD461.S7$bv.88
072 0 $aX500
082 00 $a541.2/2 s$a572/.7517$221
084 $a35.75$2bcl
084 $a35.74$2bcl
245 00 $aMetal sites in proteins and models :$biron centres /$cvolume editors, H.A.O. Hill, P.J. Sadler, A.J. Thompson ; with contributions by S.K. Chapman [and others].
260 $aBerlin ;$aNew York :$bSpringer,$c℗♭1997.
300 $aviii, 225 pages :$billustrations (some color) ;$c25 cm.
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
338 $avolume$bnc$2rdacarrier
490 1 $aStructure and bonding,$x0081-5993 ;$v88
504 $aIncludes bibliographical references and index.
505 0 $aPolyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes / A.K. Powell -- Heme: the most versatile redox centre in biology? / S.K. Chapman -- Rationalisation of metal-binding to transferrin: prediction of metal-protein stability constants / H. Sun -- Metal centres of bacterioferritins or non-heam-iron-containing cytochromes b-́́- / N.E. Le Brun -- Ribonucleotide reductases -- a group of enzymes with different metallosites and similar reaction mechanism / B.-M. Sjo berg -- Protein engineering of cytochrome P450cam / L.-L. Wong -- Author index: volumes 1-88.
650 0 $aMetalloenzymes.
650 0 $aIron proteins.
650 12 $aFerrous Compounds$xmetabolism.
650 12 $aOxidation-Reduction.
650 22 $aCytochromes$xmetabolism.
650 7 $aMe talloprote ines.$2fmesh
650 7 $aFer$xMe tabolisme.$2fmesh
650 7 $aIron proteins.$2fast$0(OCoLC)fst00979315
650 7 $aMetalloenzymes.$2fast$0(OCoLC)fst01017919
650 17 $aCytochroom P450.$2gtt
650 17 $aIJzerbindende eiwitten.$2gtt
650 17 $aFerritine.$2gtt
650 17 $aReductasen.$2gtt
650 17 $aHaem.$2gtt
650 7 $aFerroprote ines.$2ram
650 7 $aMine ralisation (biologie)$2ram
650 7 $aChimie bioinorganique.$2ram
650 7 $aFer$xCompose s.$2ram
650 7 $aMe talloenzymes.$2ram
650 07 $aEisenproteide.$2swd
650 07 $aAktives Zentrum.$2swd
650 07 $aAufsatzsammlung.$2swd
650 07 $aMetallproteide.$2swd
650 07 $aRedoxreaktion.$2swd
700 1 $aHill, H. A. O.$q(Hugh Allen Oliver)
700 1 $aSadler, P. J.
700 1 $aThompson, Andrew$q(Andrew J.)
830 0 $aStructure and bonding ;$v88.$x0081-5993
856 41 $3Table of contents$uhttp://www.gbv.de/dms/ohb-opac/232443971.pdf$zKostenfrei
856 $31850-9999$uhttp://www.springer.com/gb/$xBLDSS
938 $aBaker & Taylor$bBKTY$c206.00$d206.00$i3540628703$n0003082026$sactive
938 $aBaker and Taylor$bBTCP$n97208969
938 $aOtto Harrassowitz$bHARR$nhar005003136
938 $aYBP Library Services$bYANK$n1435441
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994 $aZ0$bP4A
948 $hNO HOLDINGS IN P4A - 133 OTHER HOLDINGS