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| [[Image:1mrr.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mrr| PDB=1mrr | SCENE= }} | | {{STRUCTURE_1mrr| PDB=1mrr | SCENE= }} |
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| '''SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION'''
| | ===SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION=== |
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| ==Overview==
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| Each polypeptide chain of protein R2, the small subunit of ribonucleotide reductase from Escherichia coli, contains a stable tyrosyl radical and two antiferromagnetically coupled oxo-bridged ferric ions. A refined structure of R2 has been recently obtained. R2 can be converted into apoR2 by chelating out the metal cofactor and scavenging the radical. This study shows that apoR2 has a very strong affinity for four stable Mn2+ ions. The manganese-containing form of R2, named Mn-R2, has been studied by EPR spectroscopy and x-ray crystallography. It contains two binuclear manganese clusters in which the two manganese ions occupy the natural iron-binding sites and are only bridged by carboxylates from glutamates 115 and 238. This in turn explains why the spin-exchange interaction between the two ions is very weak and why Mn-R2 is EPR active. Mn-R2 could provide a model for the native diferrous form of protein R2, and a detailed molecular mechanism for the reduction of the iron center of protein R2 is proposed.
| | The line below this paragraph, {{ABSTRACT_PUBMED_1328209}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 1328209 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_1328209}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Eklund, H.]] | | [[Category: Eklund, H.]] |
| [[Category: Nordlund, P.]] | | [[Category: Nordlund, P.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:38:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:40:35 2008'' |