Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Evidence for n coordination to fe in the 2fe-2s clusters of thermus rieske protein and phthalate dioxygenase from pseudomonas

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Cline, J. F.
  • Hoffman, B. M.
  • Mims, W. B.
  • Lahaie, E.
  • Ballou, D. P.
  • Fee, James

publication date

  • 1985

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Rieske-type iron/sulfur proteins and several NADH-dependent oxygenases contain Fe/S clusters with similar spectral and magnetic properties. Purified Rieske iron/sulfur protein from Thermus thermophilus contains two apparently identical [2Fe-2S] clusters in a polypeptide having only four cysteine residues, and it has been proposed that each Fe/S cluster is coordinated to two cysteine S-atoms and to an unknown number of other non-sulfur atoms (Fee, J. A., Findling, K. L., Yoshida, T., Hille, R., Tarr, G. E., Hearshen, D. O., Dunham, W. R., Day, E. P., Kent, T. A., and Munck, E. (1984) J. Biol. Chem. 259, 124-133). We have examined the Rieske protein from Thermus and the phthalate dioxygenase from Pseudomonas cepacia with electron nuclear double resonance (ENDOR) and pulsed EPR methods and report here evidence for the direct coordination of nitrogenous ligands to the Fe/S clusters in these proteins. The electron nuclear double resonance signals arising from 14N have been interpreted in terms of a strongly coupled ligand with AN = approximately 26-28 MHz and a weakly coupled ligand with AN = approximately 9 MHz. The pulsed EPR spectrum shows a rich pattern of lines in the Fourier transformed data having peaks in the range of 0.8 to 6.7 MHz. The lower frequency resonances are tentatively associated with coupling of the unpaired spin to the remote N-atoms of coordinated imidazole rings.

subject areas

  • Electron Spin Resonance Spectroscopy
  • Electron Transport Complex III
  • Iron-Sulfur Proteins
  • Oxygenases
  • Pseudomonas
  • Thermus
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 2982852
scroll to property group menus

Additional Document Info

start page

  • 3251

end page

  • 3254

volume

  • 260

issue

  • 6

©2019 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support