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Show Acetyl Coenzyme a Synthase Chemical Synthesis of a Model of the Bimetallic Active Site Victor Do It u kin (Eric L. H^yy \ Department of Chemistry, University ol Utah Th* hifunalond I enzyn wljn ban rnonoylde dehydrogenaiefacet^l-coenayme A sprttiase (fflttU AC^t pty4 di vlCdl role In dUtatrophlc COZ fhatlon tCDH caulyze* 1 he itve^iblt reduction of CCE to CO wtifeACS caid lyzei l he foirndCiOfi of aceiyl-£_oA from CQ. eoen^me A, and j rnei hyl q ir>jp. i m-il ¦ Itiesetwo isaCems playavttBl rot In the cocal q tolal lji bon t^:le.Tlie newly icived 11 ytidl HrULCUreo ACS repealed a jnlque Hl-Hl active site that we attempted Co model m ofder to shed some llghc on iht LdidlyriL . ui illztd by che tfi2yrne_ Whlfe n^rfdi n^ an salve ilie Wuh r>ne Nl atom "rt not Jihituh. buikJm^i i Inccrporatlrg boch oh he Nl acorn* his prawn to bet ctialenge for rn ukiple heseAKhers fMa fccuaed on the-devdcprnem of blnuclear rnecdl Loniplexei Otw approach rdied on apf^ndlng d chid previously known vu nii-i i m i, iikK , \ m che couse of m> reaEardi, ^ve woitedon [he lynches^ of [he new r^and employing pepcide coupling [n_ fni p^usi and NMH ipeccrO£copy_We fuve attempted several eftffarent s^irtiietlc routes Co achieve high ^fclda of pure compounds.We havealr^dhdy iymhs^iz-il and puilfied lhe h i here X = N. and we are In prtttiioriymheilioriheHgand In vrfikfi X = O_ Nt fcd Loniplexei piepaiedand characterized STr HClh I I .1 Lllllhl "Illlld11 llhT CLhLl \L limin |