Redox-linked conformational control of proton-coupled electron transfer: Y122 in the ribonucleotide reductase β2 subunit.

No abstract is available for this paper.

• Publication year

  2013

• Venue

  Journal of Physical Chemistry B

• Publication date

  2013-07-18

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/jp404757rPMID 23822111PMCID PMC3757525
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Redox-linked changes to the hydrogen-bonding network of ribonucleotide reductase β2.

  2013cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2011cited by this paper
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  2011cited by this paper
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  2011cited by this paper
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  2011cited by this paper
• Low-resolution refinement in the program REFMAC

  2011cited by this paper
• Proton coupled electron transfer and redox active tyrosines in Photosystem II.

  2011cited by this paper
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  2011cited by this paper
• HF-EPR, Raman, UV/VIS Light Spectroscopic, and DFT Studies of the Ribonucleotide Reductase R2 Tyrosyl Radical from Epstein-Barr Virus

  2011cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2009cited by this paper
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  2009cited by this paper
• Redox-linked structural changes in ribonucleotide reductase.

  2009cited by this paper
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  2008cited by this paper
• Infrared spectroscopy of proteins.

  2007cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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  2007cited by this paper
• Normal modes of redox-active tyrosine: conformation dependence and comparison to experiment.

  2006cited by this paper
• Semiempirical GGA‐type density functional constructed with a long‐range dispersion correction

  2006cited by this paper
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  2006cited by this paper
• The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

  2006cited by this paper
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  2006cited by this paper
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  2006cited by this paper
• Conformation effects on the electronic structures of beta-alanine.

  2006cited by this paper
• Redox-active tyrosine residues in pentapeptides.

  2005cited by this paper
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  2005cited by this paper
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  2003cited by this paper
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  2003cited by this paper
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  2003cited by this paper
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  2003cited by this paper
• What vibrations tell about proteins

  2002cited by this paper
• Spectroscopic properties of tyrosyl radicals in dipeptides.

  2002cited by this paper
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  2002cited by this paper
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  2001cited by this paper
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  2000cited by this paper
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  2000cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
• Protein Radicals in Enzyme Catalysis.

  1998cited by this paper
• Density functional calculations on model tyrosyl radicals.

  1997cited by this paper
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  1995cited by this paper
• Similarities and Differences between Phenoxyl and Tyrosine Phenoxyl Radical Structures, Vibrational Frequencies, and Spin Densities

  1995cited by this paper
• Reduction of the tyrosyl radical and the iron center in protein R2 of ribonucleotide reductase from mouse, herpes simplex virus and E. coli by p‐alkoxyphenols

  1995cited by this paper
• The use and misuse of FTIR spectroscopy in the determination of protein structure.

  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• EPR stopped-flow studies of the reaction of the tyrosyl radical of protein R2 from ribonucleotide reductase with hydroxyurea.

  1992cited by this paper
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  1992cited by this paper
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  1992cited by this paper
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  1992cited by this paper
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  1989cited by this paper
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  1989cited by this paper
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  1987cited by this paper
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  1982cited by this paper
• Solvent isotope effects of enzyme systems.

  1982cited by this paper
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  1978cited by this paper
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  1976cited by this paper
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  2020cites this paper
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  2018cites this paper
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  2018influential citation
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  2017cites this paper
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  2015cites this paper
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  2015cites this paper
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