Structure and function of the xanthine-oxidase family of molybdenum enzymes

M. J. Romao, R. Huber

Research output: Contribution to journalReview articlepeer-review

Abstract

This work gives an account of the recent achievements which have contributed towards the understanding of the structure and function of the xanthine oxidase family of enzymes-the molybdenum hydroxylases. It is based essentially on the crystallographic data of the aldehyde oxido-reductase from Desulfovibrio (D.) gigas, a member of that family, whose structure is described in detail. Comparisons are made, whenever appropriate, with spectroscopic, kinetic and model compound studies. Mechanistic implications of the crystal structure of the D. gigas enzyme are considered and extended to the xanthine oxidase family.
Original languageEnglish
Pages (from-to)69-95
JournalMETAL SITES IN PROTEINS AND MODELS
Volume90
Publication statusPublished - 1998

Keywords

  • hydroxylase
  • molybdoenzymes
  • molybdopterin
  • protein crystallography
  • xanthine oxidase

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