7O9D

peroxide-bound diCo-sulerythrin

Summary for 7O9D

• Entry DOI: 10.2210/pdb7o9d/pdb
• Descriptor: Sulerythrin, COBALT (II) ION, HYDROGEN PEROXIDE, ... (5 entities in total)
• Functional Keywords: sulerythrin, hydrogen peroxide, molecular oxygen, bi-metallic binding site, oxidoreductase
• Biological source: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
• Total number of polymer chains: 2
• Total formula weight: 33020.15

Authors

Jeoung, J.-H.,Dobbek, H. (deposition date: 2021-04-15, release date: 2021-12-01, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.28 Å)