Structural highlights
Function[SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedArtificial metalloproteins (ArMs) containing Co4O4 cubane active sites were constructed via biotin-streptavidin technology. Stabilized by hydrogen bonds (H-bonds), terminal and cofacial Co(III)-OH2 moieties are observed crystallographically in a series of immobilized cubane sites. Solution electrochemistry provided correlations of oxidation potential and pH. For variants containing Ser and Phe adjacent to the metallocofactor, 1e(-)/1H(+) chemistry predominates until pH 8, above which the oxidation becomes pH-independent. Installation of Tyr proximal to the Co4O4 active site provided a single H-bond to one of a set of cofacial Co(III)-OH2 groups. With this variant, multi-e(-)/multi-H(+) chemistry is observed, along with a change in mechanism at pH 9.5 that is consistent with Tyr deprotonation. With structural similarities to both the oxygen-evolving complex of photosystem II (H-bonded Tyr) and to thin film water oxidation catalysts (Co4O4 core), these findings bridge synthetic and biological systems for water oxidation, highlighting the importance of secondary sphere interactions in mediating multi-e(-)/multi-H(+) reactivity. Artificial Metalloproteins Containing Co4O4 Cubane Active Sites.,Olshansky L, Huerta-Lavorie R, Nguyen AI, Vallapurackal J, Furst A, Tilley TD, Borovik AS J Am Chem Soc. 2018 Feb 13. doi: 10.1021/jacs.7b13052. PMID:29401385[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 06:35, 17 April 2019.