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A ring-shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme–heme pocket interaction

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Abstract

Engineered cytochrome b562, a small hemoprotein, with an externally-attached heme moiety via a moderately long linker at a suitable position predominantly forms a thermodynamically stable ring-shaped trimer in dilute solution. In an equilibrium between supramolecular polymerization and depolymerization, the ring-shaped trimer is kinetically trapped even in a concentrated solution.

Graphical abstract: A ring-shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme–heme pocket interaction

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Publication details

The article was received on 22 Nov 2018, accepted on 12 Dec 2018 and first published on 12 Dec 2018


Article type: Communication
DOI: 10.1039/C8CC09314H
Citation: Chem. Commun., 2019, Advance Article
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    A ring-shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme–heme pocket interaction

    K. Oohora, R. Kajihara, N. Fujimaki, T. Uchihashi and T. Hayashi, Chem. Commun., 2019, Advance Article , DOI: 10.1039/C8CC09314H

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