Perchlorate reduction to chloride by the dimolybdenum(II) core: Making a case for molybdenum cofactor in the perchlorate reductase enzyme<i style=""></i>

Abstract

Ligand-transfer reaction from the quadruply bonded complex <i style="">cis</i>-[Mo₂(pzNP)₂(OAc)₂][BF₄]₂ (<b style="">1</b>) (pzNP = 2-(2-pyrazinyl)- 1,8-naphthyridine) to non-bonded dicopper(I) core proceeds with the concomitant oxidation of the [Mo₂]⁴⁺ core by the perchlorate anion, resulting in the [Cu₂(<img src='/image/spc_char/micro.gif' border=0> -Cl)(pzNP)₂][ClO₄] (<b style="">2</b>) and oxo-molybdenum species. X-ray analysis of (<b style="">2</b>) shows the presence of a chloride anion bridging the two Cu(I) atoms. The chloride originates from the quantitative reduction of one perchlorate anion by the electron-rich dimolybdenum(II) species, mimicking the functional role of molybolenum cofactor in the perchlorate<b style=""> </b>reducing bacteria.