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Inorganics 2016, 4(2), 12;

Advances in Engineered Hemoproteins that Promote Biocatalysis

Department of Chemistry, Benedictine University, 5700 College Road, Lisle, IL 60532, USA
Author to whom correspondence should be addressed.
Academic Editor: Duncan H. Gregory
Received: 31 March 2016 / Revised: 22 April 2016 / Accepted: 26 April 2016 / Published: 4 May 2016
(This article belongs to the Special Issue Traversing the Boundaries of Inorganic Chemistry)
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Some hemoproteins have the structural robustness to withstand extraction of the heme cofactor and replacement with a heme analog. Recent reports have reignited interest and exploration in this field by demonstrating the versatility of these systems. Heme binding proteins can be utilized as protein scaffolds to support heme analogs that can facilitate new reactivity by noncovalent bonding at the heme-binding site utilizing the proximal ligand for support. These substituted hemoproteins have the capability to enhance catalytic reactivity and functionality comparatively to their native forms. This review will focus on progress and recent advances of artificially engineered hemoproteins utilized as a new target for the development of biocatalysts. View Full-Text
Keywords: bioinorganic chemistry; hemoproteins; biocatalysts; protein scaffolds bioinorganic chemistry; hemoproteins; biocatalysts; protein scaffolds

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Stone, K.L.; Ahmed, S.M. Advances in Engineered Hemoproteins that Promote Biocatalysis. Inorganics 2016, 4, 12.

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