1h0n
From Proteopedia
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COBALT SUBSTITUTION OF MOUSE R2 RIBONUCLEOTIDE REDUCTASE TO MODEL THE REACTIVE DIFERROUS STATE
Overview
The R2 dimer of mouse ribonucleotide reductase contains a dinuclear, iron-oxygen cluster and tyrosyl radical/subunit. The dinuclear diferrous, form reacts with dioxygen to generate the tyrosyl radical essential for, the catalytic reaction that occurs at the R1 dimer. It is important to, understand how the reactivity toward oxygen is related to the crystal, structure of the dinuclear cluster. For the mouse R2 protein, no structure, has been available with a fully occupied dinuclear metal ion site. A, cobalt substitution of mouse R2 was performed to produce a good model for, the very air-sensitive diferrous form of the enzyme. X-band EPR and light, absorption studies (epsilon(550 nm) = 100 mm(-1) cm(-1)/Co(II)) revealed a, strong cooperative binding of cobalt to the dinuclear site. In, ... [(full description)]
About this Structure
1H0N is a [Single protein] structure of sequence from [Mus musculus] with CO as [ligand]. Active as [Ribonucleoside-diphosphate reductase], with EC number [1.17.4.1]. Structure known Active Site: CO1. Full crystallographic information is available from [OCA].
Reference
Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state Spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt cluster., Strand KR, Karlsen S, Andersson KK, J Biol Chem. 2002 Sep 13;277(37):34229-38. Epub 2002 Jun 26. PMID:12087093
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