Tungsten-Containing Enzymes

N. P. L'vov, A. N. Nosikov, and A. N. Antipov^*

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 117071 Russia; fax: (095) 954-2732; E-mail: lvov@mx.inbi.ras.ru

^* To whom correspondence should be addressed.

Received July 12, 2001; Revision received October 30, 2001

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The biological importance of tungsten has been fully proved in the last decade due to isolation of a number of tungsten-containing enzymes (W-enzymes) from hyperthermophilic archaea. Tungsten was previously considered only as an antagonist of molybdenum, because the replacement of molybdenum by tungsten (due to their chemical similarity) leads to inactivation of molybdenum-containing enzymes (Mo-enzymes). In addition to the “true W-enzymes” in which tungsten cannot be replaced by molybdenum, recently some enzymes have been isolated which can use either molybdenum or tungsten in the catalytic process. This review briefly summarizes data on the participation of tungsten in catalysis by some enzymes and the structure of the active sites of W-enzymes.

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KEY WORDS: tungsten, molybdenum, enzymatic catalysis, pterin cofactor

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