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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.

Publication ,  Journal Article
Madden, JF; Han, SH; Siegel, LM; Spiro, TG
Published in: Biochemistry
June 27, 1989

Resonance Raman (RR) spectra from the hemoprotein subunit of Escherichia coli sulfite reductase (SiR-HP) are examined in the low-frequency (200-500 cm-1) region where Fe-S stretching modes are expected. In spectra obtained with excitation in the siroheme Soret or Q bands, this region is dominated by siroheme modes. Modes assignable to the Fe4S4 cluster are selectively enhanced, however, with excitation at 488.0 or 457.9 nm. The assignments are confirmed by observation of the expected frequency shifts in SiR-HP extracted from E. coli grown on 34S-labeled sulfate. The mode frequencies and isotopic shifts resemble those seen in RR spectra of other Fe4S4 proteins and analogues, but the breathing mode of the cluster at 342 cm-1 is higher than that observed in the other species. Spectra of various ligand complexes of SiR-HP reveal only slight sensitivity of the cluster terminal ligand modes to the presence of exogenous heme ligands, at variance with a model of ligand binding in a bridged mode between heme and cluster. Close examination of RR spectra obtained with siroheme Soret-band excitation reveals additional 34S-sensitive features at 352 and 393 cm-1. These may be attributed to a bridging thiolate ligand.

Duke Scholars

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

June 27, 1989

Volume

28

Issue

13

Start / End Page

5471 / 5477

Location

United States

Related Subject Headings

  • Sulfur Isotopes
  • Sulfur
  • Sulfite Reductase (NADPH)
  • Spectrum Analysis, Raman
  • Protein Conformation
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Metalloproteins
  • Iron-Sulfur Proteins
  • Iron
 

Citation

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Madden, J. F., Han, S. H., Siegel, L. M., & Spiro, T. G. (1989). Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry, 28(13), 5471–5477. https://doi.org/10.1021/bi00439a023
Madden, J. F., S. H. Han, L. M. Siegel, and T. G. Spiro. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.Biochemistry 28, no. 13 (June 27, 1989): 5471–77. https://doi.org/10.1021/bi00439a023.
Madden JF, Han SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry. 1989 Jun 27;28(13):5471–7.
Madden, J. F., et al. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.Biochemistry, vol. 28, no. 13, June 1989, pp. 5471–77. Pubmed, doi:10.1021/bi00439a023.
Madden JF, Han SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. Biochemistry. 1989 Jun 27;28(13):5471–5477.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

June 27, 1989

Volume

28

Issue

13

Start / End Page

5471 / 5477

Location

United States

Related Subject Headings

  • Sulfur Isotopes
  • Sulfur
  • Sulfite Reductase (NADPH)
  • Spectrum Analysis, Raman
  • Protein Conformation
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Metalloproteins
  • Iron-Sulfur Proteins
  • Iron