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Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase.

Publication ,  Journal Article
Raitsimring, AM; Astashkin, AV; Feng, C; Enemark, JH; Nelson, KJ; Rajagopalan, KV
Published in: J Biol Inorg Chem
January 2003

Electron spin echo envelope modulation (ESEEM) spectroscopy has been used to determine the hyperfine ( hfi) and quadrupole ( nqi) interactions of the exchangeable deuteron (proton) at the Mo(V) site of DMSO reductase. The data obtained have been translated into structure-related parameters. It was found that isotropic hfi constant of the proton is not unique, but is distributed within a range of 26-36 MHz. From this hfi distribution, a 30 degrees -wide distribution of the OH bond orientations due to a rotation around the Mo-O bond was estimated. The angle between the axes of the nqi and anisotropic hfi tensors was found to be anomalously small in comparison with that expected from the Mo-O-D bond geometry. This peculiarity was attributed to the effect of spin density on the hydroxyl oxygen atom. The orientation of the Mo-OH fragment with respect to the g-frame was determined from the experimental orientations of the nqi and hfi tensor axes and a theoretical evaluation of the anisotropic hfi axis direction.

Duke Scholars

Published In

J Biol Inorg Chem

DOI

ISSN

0949-8257

Publication Date

January 2003

Volume

8

Issue

1-2

Start / End Page

95 / 104

Location

Germany

Related Subject Headings

  • Structure-Activity Relationship
  • Recombinant Proteins
  • Protons
  • Oxidoreductases
  • Molybdenum
  • Models, Molecular
  • Iron-Sulfur Proteins
  • Electron Spin Resonance Spectroscopy
  • Deuterium
  • Biophysics
 

Citation

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Chicago
ICMJE
MLA
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Raitsimring, A. M., Astashkin, A. V., Feng, C., Enemark, J. H., Nelson, K. J., & Rajagopalan, K. V. (2003). Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase. J Biol Inorg Chem, 8(1–2), 95–104. https://doi.org/10.1007/s00775-002-0393-8
Raitsimring, Arnold M., Andrei V. Astashkin, Changjian Feng, John H. Enemark, Kimberly Johnson Nelson, and K. V. Rajagopalan. “Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase.J Biol Inorg Chem 8, no. 1–2 (January 2003): 95–104. https://doi.org/10.1007/s00775-002-0393-8.
Raitsimring AM, Astashkin AV, Feng C, Enemark JH, Nelson KJ, Rajagopalan KV. Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase. J Biol Inorg Chem. 2003 Jan;8(1–2):95–104.
Raitsimring, Arnold M., et al. “Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase.J Biol Inorg Chem, vol. 8, no. 1–2, Jan. 2003, pp. 95–104. Pubmed, doi:10.1007/s00775-002-0393-8.
Raitsimring AM, Astashkin AV, Feng C, Enemark JH, Nelson KJ, Rajagopalan KV. Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase. J Biol Inorg Chem. 2003 Jan;8(1–2):95–104.
Journal cover image

Published In

J Biol Inorg Chem

DOI

ISSN

0949-8257

Publication Date

January 2003

Volume

8

Issue

1-2

Start / End Page

95 / 104

Location

Germany

Related Subject Headings

  • Structure-Activity Relationship
  • Recombinant Proteins
  • Protons
  • Oxidoreductases
  • Molybdenum
  • Models, Molecular
  • Iron-Sulfur Proteins
  • Electron Spin Resonance Spectroscopy
  • Deuterium
  • Biophysics