Kisker, Caroline and Schindelin, Hermann and Rees, Douglas C. (1997) Molybdenum-cofactor-containing enzymes: structure and mechanism. Annual Review of Biochemistry, 66 . pp. 233-267. ISSN 0066-4154. http://resolver.caltech.edu/CaltechAUTHORS:KISarb97
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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.
|Additional Information:||"Reprinted, with permission, from the Annual Review of Biochemistry, Volume 66 copyright 1997 by Annual Reviews, www.annualreviews.org" Supported by Deutsche Forschungsgemeinschaft postdoctoral fellowships (to CK and HS) and by USPHS grant GM50775 (to DCR). The authors would like to thank group members and MWW Adams, J Enemark, J Hilton, MK Johnson, and KV Rajagopalan for stimulating discussions and collaborations on Mo-co-containing enzymes.|
|Subject Keywords:||molybdopterin, molybdoenzymes, tungstoenzymes, oxotransferases, molybdenum hydroxylases|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Archive Administrator|
|Deposited On:||08 Sep 2005|
|Last Modified:||26 Dec 2012 08:40|
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