Metal Thiolate and Metal Sufide Clusters in Proteins
Savelieff, Masha Georges
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https://hdl.handle.net/2142/84319
Description
Title
Metal Thiolate and Metal Sufide Clusters in Proteins
Author(s)
Savelieff, Masha Georges
Issue Date
2008
Doctoral Committee Chair(s)
Lu, Yi
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
Finally efforts towards the design of a biosynthetic model of Cu Z from N2OR are reported. The CuZ cluster is the first and only report to date of a copper-sulfide cluster in Nature. It fulfills a catalytic role in N2OR, performing the reduction of N2O to N2 and H2O during anaerobic respiration, with reducing equivalents provided by a CuA site. The cluster is composed of four copper atoms bridged by a central sulfide, with remaining all histidine coordination to the copper atoms. A scaffold protein was selected, and residues were chosen for mutagenesis to create a similar ligand set to CuZ in N2OR. The copper binding properties and copper/sulfide binding properties of the biosynthetic and native N2OR systems were investigated towards efforts to reconstitute them.
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