MOLYBDENUM-COFACTOR–CONTAINING ENZYMES: Structure and Mechanism

Annual Review of Biochemistry - Tập 66 Số 1 - Trang 233-267 - 1997
Caroline Kisker1, Hermann Schindelin1, Douglas C. Rees1
1Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, California 91125

Tóm tắt

Molybdenum-containing enzymes catalyze basic metabolic reactions in the nitrogen, sulfur, and carbon cycles. With the exception of the nitrogenase cofactor, molybdenum is incorporated into proteins as the molybdenum cofactor that contains a mononuclear molybdenum atom coordinated to the sulfur atoms of a pterin derivative named molybdopterin. Certain microorganisms can also utilize tungsten in a similar fashion. Molybdenum-cofactor–containing enzymes catalyze the transfer of an oxygen atom, ultimately derived from or incorporated into water, to or from a substrate in a two-electron redox reaction. On the basis of sequence alignments and spectroscopic properties, four families of molybdenum-cofactor–containing enzymes have been identified. The available crystallographic structures for members of these families are discussed within the framework of the active site structure and catalytic mechanisms of molybdenum-cofactor–containing enzymes. Although the function of the molybdopterin ligand has not yet been conclusively established, interactions of this ligand with the coordinated metal are sensitive to the oxidation state, indicating that the molybdopterin may be directly involved in the enzymatic mechanism.

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Annual Review of Biochemistry

Tập 66 Số 1

233-267

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