7O9D

peroxide-bound diCo-sulerythrin

7O9D の概要

• エントリーDOI: 10.2210/pdb7o9d/pdb
• 分子名称: Sulerythrin, COBALT (II) ION, HYDROGEN PEROXIDE, ... (5 entities in total)
• 機能のキーワード: sulerythrin, hydrogen peroxide, molecular oxygen, bi-metallic binding site, oxidoreductase
• 由来する生物種: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33020.15

構造登録者

Jeoung, J.-H.,Dobbek, H. (登録日: 2021-04-15, 公開日: 2021-12-01, 最終更新日: 2024-01-31)

主引用文献

Jeoung, J.H.,Runger, S.,Haumann, M.,Neumann, B.,Klemke, F.,Davis, V.,Fischer, A.,Dau, H.,Wollenberger, U.,Dobbek, H.
Bimetallic Mn, Fe, Co, and Ni Sites in a Four-Helix Bundle Protein: Metal Binding, Structure, and Peroxide Activation.
Inorg.Chem., 60:17498-17508, 2021

PubMed Abstract: Bimetallic active sites in enzymes catalyze small-molecule conversions that are among the top 10 challenges in chemistry. As different metal cofactors are typically incorporated in varying protein scaffolds, it is demanding to disentangle the individual contributions of the metal and the protein matrix to the activity. Here, we compared the structure, properties, and hydrogen peroxide reactivity of four homobimetallic cofactors (Mn(II), Fe(II), Co(II), Ni(II)) that were reconstituted into a four-helix bundle protein. Reconstituted proteins were studied in solution and in crystals. All metals bind with high affinity and yield similar cofactor structures. Cofactor variants react with HO but differ in their turnover rates, accumulated oxidation states, and trapped peroxide-bound intermediates. Varying the metal composition thus creates opportunities to tune the reactivity of the bimetallic cofactor and to study and functionalize reactive species.

PubMed: 34757735
DOI: 10.1021/acs.inorgchem.1c01919

実験手法

X-RAY DIFFRACTION (1.28 Å)