Construction of ligand-binding controlled hemoprotein assemblies utilizing 3D domain swapping

Tsuyoshi Mashima; Masaru Yamanaka; Atsuki Yoshida; Naoya Kobayashi; Yui Kanaoka; Takayuki Uchihashi; Shun Hirota

doi:10.1039/d4cc03129f

Construction of ligand-binding controlled hemoprotein assemblies utilizing 3D domain swapping

Chem Commun (Camb). 2024 Aug 27;60(70):9440-9443. doi: 10.1039/d4cc03129f.

Authors

Tsuyoshi Mashima^{1

2}, Masaru Yamanaka¹, Atsuki Yoshida¹, Naoya Kobayashi¹, Yui Kanaoka³, Takayuki Uchihashi^{3

4}, Shun Hirota¹

Affiliations

¹ Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. [email protected].
² Medilux Research Center, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
³ Department of Physics, Nagoya University, Nagoya, 464-8602, Japan.
⁴ Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Higashiyama 5-1, Myodaiji, Okazaki, 444-0864, Japan.

PMID: 39139060
DOI: 10.1039/d4cc03129f

Abstract

Association-controllable hemoprotein assemblies were constructed from a fusion protein containing two c-type cytochrome units using 3D domain swapping. The hemoprotein assembly exhibited a dynamic exchange between cyclic and linear structures and could be regulated by carbon monoxide (CO) and imidazole binding.

MeSH terms

Binding Sites
Carbon Monoxide* / chemistry
Hemeproteins* / chemistry
Hemeproteins* / metabolism
Imidazoles* / chemistry
Ligands
Models, Molecular
Protein Binding
Protein Domains
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / genetics
Recombinant Fusion Proteins / metabolism

Substances

Ligands
Carbon Monoxide
Imidazoles
Hemeproteins
imidazole
Recombinant Fusion Proteins