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Oligomerization of cytochrome c, myoglobin, and related heme proteins by 3D domain swapping

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dc.contributor.author Hirota, Shun en
dc.date.accessioned 2019-10-03T07:38:25Z en
dc.date.available 2019-10-03T07:38:25Z en
dc.date.issued 2019-05 en
dc.identifier.issn 0162-0134 en
dc.identifier.uri http://hdl.handle.net/10061/13393 en
dc.description.abstract Oligomerization of heme proteins is useful for construction of new materials with cooperative and systematic functions; thus, diverse methods have been applied for construction of artificial heme protein oligomers. Three-dimensional (3D) domain swapping is a protein oligomerization phenomenon that exchanges the same domain or secondary structural element between molecules. 3D domain swapping was first reported in 1994; since then many proteins have been reported to domain swap. Our research group has been showing that various heme proteins domain swap. We also found that domain swapping of heme proteins occurs at the early stage of protein folding, and utilized it to construct various heme protein assemblies, including nanorings, cages, hetero dimers with different active sites, and a ligand-binding reversible monomer–polymer system. In this review, the basics and applications of domain swapping of heme proteins are summarized. ja
dc.language.iso en en
dc.publisher Elsevier en
dc.rights © 2019 Elsevier Inc. All rights reserved. 出版社許諾条件により、本文は2021年5月1日以降に公開 ja
dc.title Oligomerization of cytochrome c, myoglobin, and related heme proteins by 3D domain swapping en
dc.type.nii Journal Article en
dc.contributor.transcription ヒロタ, シュン ja
dc.contributor.alternative 廣田, 俊 ja
dc.textversion author en
dc.identifier.jtitle Journal of Inorganic Biochemistry en
dc.identifier.volume 194 ja
dc.identifier.spage 170 en
dc.identifier.epage 179 en
dc.relation.doi 10.1016/j.jinorgbio.2019.03.002 en
dc.identifier.NAIST-ID 73293425 en

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