Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy

Inorg Chem. 2009 May 4;48(9):3913-5. doi: 10.1021/ic802355y.

Abstract

W-band (95 GHz) HYSCORE and pulse ENDOR are used to characterize the nitrosyl d(1) heme complex (d(1)NO) of cd(1) nitrite reductase from Pseudomonas aeruginosa in the wild type and the Y10F mutant. The spectra and the derived (14)N hyperfine and quadrupole interactions were found to be the same for wt and Y10F. This suggests that Tyr10 does not influence the NO ligand orientation in the reduced state in solution. This study is the first application of HYSCORE at high fields and shows its potential for characterizing low gamma nuclei with large hyperfine couplings.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Crystallization
  • Cytochromes / chemistry*
  • Cytochromes / genetics*
  • Cytochromes / metabolism
  • Electron Spin Resonance Spectroscopy
  • Heme / analogs & derivatives*
  • Heme / chemistry
  • Heme / metabolism
  • Ligands
  • Nitric Oxide / chemistry*
  • Nitric Oxide / metabolism
  • Nitrite Reductases / chemistry*
  • Nitrite Reductases / genetics*
  • Nitrite Reductases / metabolism
  • Protein Binding
  • Protein Conformation
  • Pseudomonas aeruginosa / enzymology*
  • Pseudomonas aeruginosa / genetics
  • Tyrosine / chemistry

Substances

  • Bacterial Proteins
  • Cytochromes
  • Ligands
  • Nitric Oxide
  • Tyrosine
  • Heme
  • heme d1
  • Nitrite Reductases
  • nitrite reductase (NO-forming)