Generation of New Artificial Metalloproteins by Cofactor Modification of Native Hemoproteins. Issue 1 (20th November 2014)

• Record Type: Journal Article
• Authors: Hayashi, Takashi; Sano, Yohei; Onoda, Akira
• Is Part Of: Israel journal of chemistry. Volume 55:Issue 1(2015)
• Page Start: 76
• Page End: 84
• Publication Date: 2014-11-20
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1002/ijch.201400123
• Languages: English
• ISSNs: 0021-2148

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Heme can be removed from a number of native hemoproteins, thus forming corresponding apoproteins, each of which provides a site for binding of a metal complex. In one example, myoglobin, an O₂ storage protein, can be reconstituted with iron porphycene to dramatically enhance the O₂ affinity. Although it is known that myoglobin has poor enzymatic activity, the insertion of iron corrole or iron porphycene into apomyoglobin increases its H₂O₂‐dependent peroxidase/peroxygenase activities. Furthermore, reconstitution with manganese porphycene promotes hydroxylation of an inert CH bond. It is also of interest to insert a non‐porphyrinoid complex into an apoprotein. A cavity of apocytochrome <italic>c</italic> has been found to bind a diiron carbonyl complex, serving as a functional model of diiron hydrogenase. Aponitrobindin has a rigid β‐barrel structure that provides an excellent cavity for covalently anchoring a metal complex. A rhodium complex embedded in the cavity of genetically modified nitrobindin has been found to promote stereoselective polymerization of phenylacetylene.</p> </abstract>