Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase
نویسندگان
چکیده
منابع مشابه
The tyrosyl free radical in ribonucleotide reductase.
The enzyme, ribonucleotide reductase, catalyses the formation of deoxyribonucleotides from ribonucleotides, a reaction essential for DNA synthesis in all living cells. The Escherichia coli ribonucleotide reductase, which is the prototype of all known eukaryotic and virus-coded enzymes, consists of two nonidentical subunits, proteins B1 and B2. The B2 subunit contains an antiferromagnetically co...
متن کاملPhotochemical Generation of a Tryptophan Radical within the Subunit Interface of Ribonucleotide Reductase.
The Escherichia coli class Ia ribonucleotide reductase (RNR) achieves forward and reverse proton-coupled electron transfer (PCET) over a pathway of redox active amino acids (β-Y122 ⇌ β-Y356 ⇌ α-Y731 ⇌ α-Y730 ⇌ α-C439) spanning ∼35 Å and two subunits every time it turns over. We have developed photoRNRs that allow radical transport to be phototriggered at tyrosine (Y) or fluorotyrosine (FnY) res...
متن کاملA tyrosine–tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette
In class 1a ribonucleotide reductase (RNR), a substrate-based radical is generated in the α2 subunit by long-distance electron transfer involving an essential tyrosyl radical (Y122O·) in the β2 subunit. The conserved W48 β2 is ∼10 Å from Y122OH; mutations at W48 inactivate RNR. Here, we design a beta hairpin peptide, which contains such an interacting tyrosine-tryptophan dyad. The NMR structure...
متن کاملCharacterization of the free radical of mammalian ribonucleotide reductase.
Mouse fibroblast 3T6 cells, selected for resistance to hydroxyurea, were shown to overproduce protein M2, one of the two nonidentical subunits of mammalian ribonucleotide reductase. Packed resistant cells gave an EPR signal at 77 K very much resembling the signal given by the tyrosine-free radical of the B2 subunit of Escherichia coli ribonucleotide reductase. Also, the M2-specific free radical...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2017
ISSN: 0002-7863,1520-5126
DOI: 10.1021/jacs.7b08192