Molybdenum and tungsten enzymes: the xanthine oxidase family

Research output: Contribution to journalReview article

79 Citations (Scopus)

Abstract

Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.

Original languageEnglish
Pages (from-to)109-114
Number of pages6
JournalCurrent Opinion in Chemical Biology
Volume10
Issue number2
DOIs
Publication statusPublished - 1 Apr 2006

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Tungsten
Molybdenum
Xanthine Oxidase
Catalytic Domain
Enzymes
Electrons
Oxygen
Atoms
Substrates

Cite this

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title = "Molybdenum and tungsten enzymes: the xanthine oxidase family",
abstract = "Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.",
author = "Brondino, {Carlos D.} and Rom{\~a}o, {Maria Jo{\~a}o} and Isabel Moura and Moura, {Jos{\'e} J. G.}",
note = "CDB and JJGM thank SECYT (Argentina) and GRICES (Portugal) for a bi-national grant. Work supported by projects EC HPRN-CT-1999-00084, POCTI/1999/BME/35078, and POCTI/1999/BME/36152 in Portugal, and SEPCYT:PICT 2003-06-13872, CONICET PIP 02559/2000 and CAI+ d- UNL in Argentina. CDB is a member of CONICET-Argentina.",
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Molybdenum and tungsten enzymes: the xanthine oxidase family. / Brondino, Carlos D.; Romão, Maria João; Moura, Isabel; Moura, José J. G.

In: Current Opinion in Chemical Biology, Vol. 10, No. 2, 01.04.2006, p. 109-114.

Research output: Contribution to journalReview article

TY - JOUR

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AU - Brondino, Carlos D.

AU - Romão, Maria João

AU - Moura, Isabel

AU - Moura, José J. G.

N1 - CDB and JJGM thank SECYT (Argentina) and GRICES (Portugal) for a bi-national grant. Work supported by projects EC HPRN-CT-1999-00084, POCTI/1999/BME/35078, and POCTI/1999/BME/36152 in Portugal, and SEPCYT:PICT 2003-06-13872, CONICET PIP 02559/2000 and CAI+ d- UNL in Argentina. CDB is a member of CONICET-Argentina.

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N2 - Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.

AB - Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.

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