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Generation of New Artificial Metalloproteins by Cofactor Modification of Native Hemoproteins
Author(s) -
Hayashi Takashi,
Sano Yohei,
Onoda Akira
Publication year - 2015
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201400123
Subject(s) - chemistry , hemeprotein , myoglobin , heme , cofactor , hemin , metalloprotein , hydrogenase , hydroxylation , combinatorial chemistry , stereochemistry , metal , enzyme , organic chemistry
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 O 2 storage protein, can be reconstituted with iron porphycene to dramatically enhance the O 2 affinity. Although it is known that myoglobin has poor enzymatic activity, the insertion of iron corrole or iron porphycene into apomyoglobin increases its H 2 O 2 ‐dependent peroxidase/peroxygenase activities. Furthermore, reconstitution with manganese porphycene promotes hydroxylation of an inert CH bond. It is also of interest to insert a non‐porphyrinoid complex into an apoprotein. A cavity of apocytochrome c 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.