Dinuclear Metalloenzymes– Structure, Function, and NMR Spectroscopy

Li-June Ming
Department of Chemistry and
Institute for Biomolecular Science
University of South Florida
Tampa, FL 33620-5250

Abstract
    Although most metalloproteins contain just mononuclear metal centers, there are a number of functionally diverse metalloproteins which possess multinuclear metal centers.  In most multinuclear metalloenzymes, the metal ions act cooperatively to afford full enzymatic activities where removal or substitution of any one metal ion may result in a change of the activities, such as in the case of aminopeptidase and Bacillus phosphotidylcholine-specific phospholipase C.  Nevertheless, there are still some multinuclear metalloenzymes, including Cu,Zn superoxide dismutase and purple acid phosphatase, whose activities may not be affected by partial removal or substitution of the metal ions (i.e., Zn(II) and Fe(II), respectively).  In this review, structural and mechanistic studies of these metalloenzymes and their paramagnetic metal-substituted derivatives by the use of 2D NMR techniques are discussed.

(This article was written in Chinese.  A more thorough review on this subject can be found in my recent review.)

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