Domain-swapped cytochrome cb 562 dimer and its nanocage encapsulating a Zn–SO4 cluster in the internal cavity† †Electronic supplementary information (ESI) available: Experimental procedure, size exclusion chromatogram, DSC thermogram, protein structure and statistics of data collection. See DOI: 10.1039/c5sc02428e Click here for additional data file.
نویسندگان
چکیده
Domain-swapped Cytochrome cb562 Dimer and Its Nanocage Encapsulating a Zn-SO4 Cluster in the Internal Cavity Takaaki Miyamoto,a Mai Kuribayashi,a Satoshi Nagao,a Yasuhito Shomura,b Yoshiki Higuchi,cdand Shun Hirota*a a Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan b Graduate School of Science and Engineering, Ibaraki University, 4-12-1, Nakanarusawa, Hitachi, Ibaraki 316-8511, Japan c Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan d RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan
منابع مشابه
Domain-swapped cytochrome cb562 dimer and its nanocage encapsulating a Zn-SO4 cluster in the internal cavity.
Protein nanostructures have been gaining in interest, along with developments in new methods for construction of novel nanostructures. We have previously shown that c-type cytochromes and myoglobin form oligomers by domain swapping. Herein, we show that a four-helix bundle protein cyt cb562, with the cyt b562 heme attached to the protein moiety by two Cys residues insertion, forms a domain-swap...
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