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1piz

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[[Image:1piz.jpg|left|200px]]
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{{STRUCTURE_1piz| PDB=1piz | SCENE= }}
{{STRUCTURE_1piz| PDB=1piz | SCENE= }}
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'''RIBONUCLEOTIDE REDUCTASE R2 D84E MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH'''
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===RIBONUCLEOTIDE REDUCTASE R2 D84E MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH===
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==Overview==
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The R2 subunit of Escherichia coli ribonucleotide reductase contains a dinuclear iron center that generates a catalytically essential stable tyrosyl radical by one electron oxidation of a nearby tyrosine residue. After acquisition of Fe(II) ions by the apo protein, the resulting diiron(II) center reacts with O(2) to initiate formation of the radical. Knowledge of the structure of the reactant diiron(II) form of R2 is a prerequisite for a detailed understanding of the O(2) activation mechanism. Whereas kinetic and spectroscopic studies of the reaction have generally been conducted at pH 7.6 with reactant produced by the addition of Fe(II) ions to the apo protein, the available crystal structures of diferrous R2 have been obtained by chemical or photoreduction of the oxidized diiron(III) protein at pH 5-6. To address this discrepancy, we have generated the diiron(II) states of wildtype R2 (R2-wt), R2-D84E, and R2-D84E/W48F by infusion of Fe(II) ions into crystals of the apo proteins at neutral pH. The structures of diferrous R2-wt and R2-D48E determined from these crystals reveal diiron(II) centers with active site geometries that differ significantly from those observed in either chemically or photoreduced crystals. Structures of R2-wt and R2-D48E/W48F determined at both neutral and low pH are very similar, suggesting that the differences are not due solely to pH effects. The structures of these "ferrous soaked" forms are more consistent with circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopic data and provide alternate starting points for consideration of possible O(2) activation mechanisms.
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(as it appears on PubMed at http://www.pubmed.gov), where 14677973 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14677973}}
==About this Structure==
==About this Structure==
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[[Category: Diferrous cluster]]
[[Category: Diferrous cluster]]
[[Category: Four helix bundle]]
[[Category: Four helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:08:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:33:43 2008''

Revision as of 11:33, 27 July 2008

Image:1piz.png

Template:STRUCTURE 1piz

RIBONUCLEOTIDE REDUCTASE R2 D84E MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH

Template:ABSTRACT PUBMED 14677973

About this Structure

1PIZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2., Voegtli WC, Sommerhalter M, Saleh L, Baldwin J, Bollinger JM Jr, Rosenzweig AC, J Am Chem Soc. 2003 Dec 24;125(51):15822-30. PMID:14677973

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