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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.

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

Resonance Raman (RR) spectra are reported for the hemoprotein subunit (SiR-HP) of Escherichia coli NADPH-sulfite reductase (EC 1.8.1.2) in various ligation and redox states. Comparison of the RR spectra of extracted siroheme and the mu-oxo FeIII dimer of octaethylisobacteriochlorin with those of mu-oxo FeIII octaethylchlorin dimer and mu-oxo FeIII octaethylporphyrin dimer demonstrates that many siroheme bands can be correlated with established porphyrin skeletal modes. Depolarization measurements are a powerful tool in this correlation, since the 45 degrees rotation of the C2 symmetry axis of the isobacteriochlorin ring relative to the chlorin system results in reversal of the polarization properties (polarized vs anomalously polarized) of bands correlating with B1g and B2g modes of porphyrin. Various SiR-HP adducts (CO, NO, CN-, SO3(2-] show upshifted high-frequency bands, characteristic of the low-spin state and consistent with the expected core size sensitivity of the skeletal modes. Fully reduced unliganded SiR-HP (both siroheme and Fe4S4 cluster reduced) in liquid solution displays RR features comparable to those of high-spin ferrous porphyrins; on freezing, the RR spectrum changes, reflecting an apparent mixture of siroheme spin states. At intermediate reduction levels in solution a RR species is observed whose high-frequency bands are upshifted relative to oxidized and fully reduced SiR-HP. This spectrum, thought to arise from the "one-electron" state of SiR-HP (siroheme reduced, cluster oxidized), may be due to S = 1 FeII siroheme.

Duke Scholars

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

June 27, 1989

Volume

28

Issue

13

Start / End Page

5461 / 5471

Location

United States

Related Subject Headings

  • Sulfite Reductase (NADPH)
  • Spectrum Analysis, Raman
  • Protein Conformation
  • Porphyrins
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Oxidation-Reduction
  • Macromolecular Substances
  • Hemeproteins
  • Heme
 

Citation

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Han, S. H., Madden, J. F., Thompson, R. G., Strauss, S. H., Siegel, L. M., & Spiro, T. G. (1989). Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry, 28(13), 5461–5471. https://doi.org/10.1021/bi00439a022
Han, S. H., J. F. Madden, R. G. Thompson, S. H. Strauss, L. M. Siegel, and T. G. Spiro. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.Biochemistry 28, no. 13 (June 27, 1989): 5461–71. https://doi.org/10.1021/bi00439a022.
Han SH, Madden JF, Thompson RG, Strauss SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry. 1989 Jun 27;28(13):5461–71.
Han, S. H., et al. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.Biochemistry, vol. 28, no. 13, June 1989, pp. 5461–71. Pubmed, doi:10.1021/bi00439a022.
Han SH, Madden JF, Thompson RG, Strauss SH, Siegel LM, Spiro TG. Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry. 1989 Jun 27;28(13):5461–5471.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

June 27, 1989

Volume

28

Issue

13

Start / End Page

5461 / 5471

Location

United States

Related Subject Headings

  • Sulfite Reductase (NADPH)
  • Spectrum Analysis, Raman
  • Protein Conformation
  • Porphyrins
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Oxidation-Reduction
  • Macromolecular Substances
  • Hemeproteins
  • Heme