Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11234
Title: Perchlorate reduction to chloride by the dimolybdenum(II) core: Making a case for molybdenum cofactor in the perchlorate reductase enzyme<i style=""></i>
Authors: Majumdar, Moumita
Bera, Jitendra K
Keywords: Bioinorganic chemistry
Perchlorate reduction
Ligand transfer reactions
Molybdenum cofactor
Dimolybdenum
Oxomolybdenum
Copper
Issue Date: Mar-2011
Publisher: NISCAIR-CSIR, India
Abstract: Ligand-transfer reaction from the quadruply bonded complex <i style="">cis</i>-[Mo<sub>2</sub>(pzNP)<sub>2</sub>(OAc)<sub>2</sub>][BF<sub>4</sub>]<sub>2</sub> (<b style="">1</b>) (pzNP = 2-(2-pyrazinyl)- 1,8-naphthyridine) to non-bonded dicopper(I) core proceeds with the concomitant oxidation of the [Mo<sub>2</sub>]<sup>4+</sup> core by the perchlorate anion, resulting in the [Cu<sub>2</sub>(<img src='/image/spc_char/micro.gif' border=0> -Cl)(pzNP)<sub>2</sub>][ClO<sub>4</sub>] (<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.
Description: 409-413
URI: http://hdl.handle.net/123456789/11234
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections:IJC-A Vol.50A(03-04) [March-April 2011]

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