Thermodynamically controlled supramolecular polymerization of cytochrome b 562.
A hemoprotein-based supramolecular polymer that has a covalently linked heme moiety on the protein surface has been constructed based on interprotein heme-heme pocket interactions of the chemically modified apocytochrome b(562) (1-H63C). The thermodynamic properties of the polymer have been investigated by means of size exclusion chromatography, UV-vis spectroscopy, and circular dichroism spectroscopy. The results indicate that, as with other synthetic systems reported so far, the 1-H63C hemoprotein assembly is thermodynamically controlled in aqueous solution: the degree of polymerization is dependent on the 1-H63C concentration and is modulated by the addition of the end-capping units, native heme, and/or apocytochrome b(562) mutant (apoH63C). These properties suggest a potential use for the hemoprotein self-assembly in preparation of stimuli-responsive functional nanobiomaterials.
Kitagishi
Hiroaki
H
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan.
Oohora
Koji
K
Hayashi
Takashi
T
D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D002942:Circular Dichroism; D045303:Cytochromes b / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D001704:Biopolymers; D045303:Cytochromes b