Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics

Larrabee, James A., Schenk, Gerhard, Mitic, Natasa and Riley, Mark J. (2015) Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics. European Biophysics Journal, 44 6: 393-415. doi:10.1007/s00249-015-1053-6


Author Larrabee, James A.
Schenk, Gerhard
Mitic, Natasa
Riley, Mark J.
Title Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics
Journal name European Biophysics Journal   Check publisher's open access policy
ISSN 1432-1017
0175-7571
Publication date 2015-09
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1007/s00249-015-1053-6
Volume 44
Issue 6
Start page 393
End page 415
Total pages 23
Place of publication Heidelberg, Germany
Publisher Springer
Collection year 2016
Language eng
Abstract Magnetic circular dichroism (MCD) is a convenient technique for providing structural and mechanistic insight into enzymatic systems in solution. The focus of this review is on aspects of geometric and electronic structure that can be determined by MCD, and how this method can further our understanding of enzymatic mechanisms. Dinuclear Co(II) systems that catalyse hydrolytic reactions were selected to illustrate the approach. These systems all contain active sites with similar structures consisting of two Co(II) ions bridged by one or two carboxylates and a water or hydroxide. In most of these active sites one Co(II) is five-coordinate and one is six-coordinate, with differing binding affinities. It is shown how MCD can be used to determine which binding site—five or six-coordinate—has the greater affinity. Importantly, zero-field-splitting data and magnetic exchange coupling constants may be determined from the temperature and field dependence of MCD data. The relevance of these data to the function of the enzymatic systems is discussed.
Keyword Biomimetics
Co(II)
Dinuclear metallohydrolases
Magnetic circular dichroism
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
 
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