Literature DB >> 10089321

Crystallization and preliminary x-ray analysis of a nitrate reductase from Desulfovibrio desulfuricans ATCC 27774.

J M Dias1, S Bursakov, C Carneiro, J J Moura, I Moura, M J Romão.   

Abstract

Periplasmic nitrate reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 contains two molybdopterin guanine dinucleotide cofactors and one [4Fe-4S] cluster as prosthetic groups and catalyzes the conversion of nitrate to nitrite. Crystals of the oxidized form of this enzyme were obtained using PEG as precipitant and belong to space group P3121 or P3221, with unit-cell dimensions a = b = 106.3, c = 135.1 A. There is one monomer of 80 kDa in the asymmetric unit, which corresponds to a Matthews ratio of 2.75 A3 Da-1. Using cryo-cooling procedures and X-rays from a rotating-anode generator, diffraction was observed to beyond 3.0 A resolution.

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Year:  1999        PMID: 10089321     DOI: 10.1107/s0907444998014735

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum.

Authors:  Shabir Najmudin; Pablo J González; José Trincão; Catarina Coelho; Abhik Mukhopadhyay; Nuno M F S A Cerqueira; Carlos C Romão; Isabel Moura; José J G Moura; Carlos D Brondino; Maria J Romão
Journal:  J Biol Inorg Chem       Date:  2008-03-08       Impact factor: 3.358

  1 in total

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