CRYSTALLOGRAPHIC INVESTIGATIONS OF THE TRYPTOPHAN-DERIVED COFACTOR IN THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE

LY CHEN, FS MATHEWS, VL DAVIDSON, EG HUIZINGA, FMD VELLIEUX, JA DUINE, WGJ HOL

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Abstract

A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase form Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.

Original languageEnglish
Pages (from-to)163-166
Number of pages4
JournalFEBS Letters
Volume287
Issue number1-2
Publication statusPublished - 5-Aug-1991

Keywords

  • METHYLAMINE DEHYDROGENASE
  • QUINOPROTEIN
  • REDOX COFACTOR
  • TRYPTOPHAN TRYPTOPHYLQUINONE
  • PYRROLOQUINOLINE QUINONE
  • AMINO ACID-DERIVED COFACTOR
  • PARACOCCUS-DENITRIFICANS
  • PURIFICATION
  • ENZYMES
  • SUBUNIT
  • GENE
  • AM1

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