Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding

Milton E. Blackwood, Thomas S. Rush, Amy Elizabeth Medlock, Harry A. Dailey, Thomas G. Spiro

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Ferrochelatase catalyzes Fe2+ insertion into porphyrins, and is inhibited by Hg2+. Resonance Raman spectra of mesoporphyrin IX show that binding to ferrochelatase restricts the conformation of the propionate side chains, but does not perturb the ring conformation. However, a pronounced perturbation is seen in the ternary complex with Hg2+. Several additional RR bands are activated, including some arising from [R-active vibrations, establishing loss of an effective symmetry center. Out-of-plane modes appear in the low frequency region. The strongest of these bands, γ5 and γ6, correspond to pyrrole tilting vibrations, which are in the same symmetry class as a doming distortion of the porphyrin. All four pyrrole N atoms are pointing toward the same side of the porphyrin plane, a geometry expected to facilitate Fe2+ insertion. This distortion is proposed to result from occupation of a metal-binding site, proximate to the prophyrin, which promotes insertion of Fe2+, while occupation by Hg2+ is inhibitory.

Original languageEnglish (US)
Pages (from-to)12170-12174
Number of pages5
JournalJournal of the American Chemical Society
Volume119
Issue number50
DOIs
StatePublished - Dec 17 1997

Fingerprint

Ferrochelatase
Porphyrins
Raman scattering
Pyrroles
Metals
Vibration
Occupations
Conformations
Propionates
Binding sites
Binding Sites
Atoms
Geometry

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Blackwood, M. E., Rush, T. S., Medlock, A. E., Dailey, H. A., & Spiro, T. G. (1997). Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding. Journal of the American Chemical Society, 119(50), 12170-12174. https://doi.org/10.1021/ja971619c

Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding. / Blackwood, Milton E.; Rush, Thomas S.; Medlock, Amy Elizabeth; Dailey, Harry A.; Spiro, Thomas G.

In: Journal of the American Chemical Society, Vol. 119, No. 50, 17.12.1997, p. 12170-12174.

Research output: Contribution to journalArticle

Blackwood, ME, Rush, TS, Medlock, AE, Dailey, HA & Spiro, TG 1997, 'Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding', Journal of the American Chemical Society, vol. 119, no. 50, pp. 12170-12174. https://doi.org/10.1021/ja971619c
Blackwood, Milton E. ; Rush, Thomas S. ; Medlock, Amy Elizabeth ; Dailey, Harry A. ; Spiro, Thomas G. / Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding. In: Journal of the American Chemical Society. 1997 ; Vol. 119, No. 50. pp. 12170-12174.
@article{74a354c7873440618ef849203a86bd54,
title = "Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding",
abstract = "Ferrochelatase catalyzes Fe2+ insertion into porphyrins, and is inhibited by Hg2+. Resonance Raman spectra of mesoporphyrin IX show that binding to ferrochelatase restricts the conformation of the propionate side chains, but does not perturb the ring conformation. However, a pronounced perturbation is seen in the ternary complex with Hg2+. Several additional RR bands are activated, including some arising from [R-active vibrations, establishing loss of an effective symmetry center. Out-of-plane modes appear in the low frequency region. The strongest of these bands, γ5 and γ6, correspond to pyrrole tilting vibrations, which are in the same symmetry class as a doming distortion of the porphyrin. All four pyrrole N atoms are pointing toward the same side of the porphyrin plane, a geometry expected to facilitate Fe2+ insertion. This distortion is proposed to result from occupation of a metal-binding site, proximate to the prophyrin, which promotes insertion of Fe2+, while occupation by Hg2+ is inhibitory.",
author = "Blackwood, {Milton E.} and Rush, {Thomas S.} and Medlock, {Amy Elizabeth} and Dailey, {Harry A.} and Spiro, {Thomas G.}",
year = "1997",
month = "12",
day = "17",
doi = "10.1021/ja971619c",
language = "English (US)",
volume = "119",
pages = "12170--12174",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "50",

}

TY - JOUR

T1 - Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding

AU - Blackwood, Milton E.

AU - Rush, Thomas S.

AU - Medlock, Amy Elizabeth

AU - Dailey, Harry A.

AU - Spiro, Thomas G.

PY - 1997/12/17

Y1 - 1997/12/17

N2 - Ferrochelatase catalyzes Fe2+ insertion into porphyrins, and is inhibited by Hg2+. Resonance Raman spectra of mesoporphyrin IX show that binding to ferrochelatase restricts the conformation of the propionate side chains, but does not perturb the ring conformation. However, a pronounced perturbation is seen in the ternary complex with Hg2+. Several additional RR bands are activated, including some arising from [R-active vibrations, establishing loss of an effective symmetry center. Out-of-plane modes appear in the low frequency region. The strongest of these bands, γ5 and γ6, correspond to pyrrole tilting vibrations, which are in the same symmetry class as a doming distortion of the porphyrin. All four pyrrole N atoms are pointing toward the same side of the porphyrin plane, a geometry expected to facilitate Fe2+ insertion. This distortion is proposed to result from occupation of a metal-binding site, proximate to the prophyrin, which promotes insertion of Fe2+, while occupation by Hg2+ is inhibitory.

AB - Ferrochelatase catalyzes Fe2+ insertion into porphyrins, and is inhibited by Hg2+. Resonance Raman spectra of mesoporphyrin IX show that binding to ferrochelatase restricts the conformation of the propionate side chains, but does not perturb the ring conformation. However, a pronounced perturbation is seen in the ternary complex with Hg2+. Several additional RR bands are activated, including some arising from [R-active vibrations, establishing loss of an effective symmetry center. Out-of-plane modes appear in the low frequency region. The strongest of these bands, γ5 and γ6, correspond to pyrrole tilting vibrations, which are in the same symmetry class as a doming distortion of the porphyrin. All four pyrrole N atoms are pointing toward the same side of the porphyrin plane, a geometry expected to facilitate Fe2+ insertion. This distortion is proposed to result from occupation of a metal-binding site, proximate to the prophyrin, which promotes insertion of Fe2+, while occupation by Hg2+ is inhibitory.

UR - http://www.scopus.com/inward/record.url?scp=2642621590&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2642621590&partnerID=8YFLogxK

U2 - 10.1021/ja971619c

DO - 10.1021/ja971619c

M3 - Article

AN - SCOPUS:2642621590

VL - 119

SP - 12170

EP - 12174

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 50

ER -