Abstract
The enzyme ribonucleotide reductase furnishes precursors for the DNA synthesis of all living cells. One of its constituents, the free radical protein, has an unusual alpha-helical structure. There are two iron centres that are about 25 A apart in the dimeric molecule. Tyrosine 122, which harbours the stable free radical necessary for the activity of ribonucleotide reductase, is buried inside the protein and is located 5 A from the closest iron atom.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Crystallization
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Escherichia coli / analysis*
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Free Radicals*
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Hemerythrin
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Iron
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Macromolecular Substances
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Molecular Sequence Data
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Molecular Structure
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Protein Conformation
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Proteins*
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Ribonucleotide Reductases*
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Sequence Homology, Nucleic Acid
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Tyrosine
Substances
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Free Radicals
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Hemerythrin
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Macromolecular Substances
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Proteins
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Tyrosine
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Iron
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Ribonucleotide Reductases