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Chemically Programmed Supramolecular Assembly of Hemoprotein and Streptavidin with Alternating Alignment
Author(s) -
Oohora Koji,
Burazerovic Sabina,
Onoda Akira,
Wilson Yvonne M.,
Ward Thomas R.,
Hayashi Takashi
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201107067
Subject(s) - streptavidin , supramolecular chemistry , hemeprotein , heme , nanotechnology , supramolecular assembly , chemistry , materials science , crystallography , biochemistry , biotin , crystal structure , enzyme
Alternating : A cofactor dyad consisting of a heme group (red in picture) and a bis(biotin) unit (blue) was synthesized and shown to specifically bind to both apomyoglobin and streptavidin. In the presence of the dyad, the 1:1 association of a disulfide‐bridged myoglobin dimer (green) with streptavidin (gray) afforded a submicrometer‐sized fibrous alternating copolymer.