期刊
COORDINATION CHEMISTRY REVIEWS
卷 257, 期 1, 页码 3-26出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2012.05.021
关键词
Ribonucleotide reductase; R2 subunit; Di-iron metal cluster; Di-manganese metal cluster; Electron paramagnetic resonance (EPR); Resonance Raman (rRaman); Circular dichroism/magnetic circular dichroism (CD/MCD); Density functional theory (DFT); SQUID magnetic measurement
资金
- Research Council of Norway [177661/V30, 214239/F20, 165716/V40, 179513, 186406/V40]
- Norwegian Cancer Society [539012]
- European Community [PIEF-GA-2009-235237]
- Operational Program Research and Development for Innovations - European Regional Fund [CZ.1.05/2.1.00/03.0058]
- Grant Agency of the Academy of Sciences of the Czech Republic [KAN115600801]
- National Science Foundation (USA) [NSF MCB 0919027]
Ribonucleotide reductase (RNR) catalyzes the rate limiting step in DNA synthesis where ribonucleotides are reduced to their corresponding deoxyribonucleotides. They are formed through a radical-induced reduction of ribonucleotides. Three classes of RNR generate the catalytically active site thiyl radical using different co-factors: a tyrosyl-radical in most cases (class I), homolytic cleavage of deoxyadenosyl-cobalamin (class II), or a glycyl-radical (class III), respectively. Class I RNR has a larger subunit R1/R1E containing the active site and a smaller subunit R2/R2F with (the thiyl-generating power from) a tyrosyl radical or an oxidized iron-manganese cluster and is reviewed herein. Class I is divided into subclasses, Ia (tyrosyl-radical and di-iron-oxygen cluster), Ib (tyrosyl-radical and di-manganese-oxygen cluster) and Ic (an iron-manganese cluster). Presented here is an overview of recent developments in the understanding of class I RNR: metal-ion cluster identities, novel 3D structures, magnetic-optical properties, and reaction mechanisms. It became clear in the last years that the primitive bacterial RNR sources can utilize different metal-ion clusters to fulfil function. Within class la that includes members from eukaryotes (mammalians, fish) and some viruses species, the presence of hydrogen bonding interactions from water at different distances with the tyrosyl-radical site can occur. This demonstrates a large versatility in the mechanism to form the thiyl radical. (C) 2012 Elsevier B.V. All rights reserved.
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