Picosecond time-resolved resonance Raman studies of hemoglobin

Implications for reactivity

E. W. Findsen, Joel M. Friedman, M. R. Ondrias, S. R. Simon

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (νFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.

Original languageEnglish (US)
Pages (from-to)661-665
Number of pages5
JournalScience
Volume229
Issue number4714
StatePublished - 1985
Externally publishedYes

Fingerprint

Hemoglobins
Iron
Histidine
Genetic Recombination
Ligands
Proteins
deoxyhemoglobin

ASJC Scopus subject areas

  • General

Cite this

Findsen, E. W., Friedman, J. M., Ondrias, M. R., & Simon, S. R. (1985). Picosecond time-resolved resonance Raman studies of hemoglobin: Implications for reactivity. Science, 229(4714), 661-665.

Picosecond time-resolved resonance Raman studies of hemoglobin : Implications for reactivity. / Findsen, E. W.; Friedman, Joel M.; Ondrias, M. R.; Simon, S. R.

In: Science, Vol. 229, No. 4714, 1985, p. 661-665.

Research output: Contribution to journalArticle

Findsen, EW, Friedman, JM, Ondrias, MR & Simon, SR 1985, 'Picosecond time-resolved resonance Raman studies of hemoglobin: Implications for reactivity', Science, vol. 229, no. 4714, pp. 661-665.
Findsen, E. W. ; Friedman, Joel M. ; Ondrias, M. R. ; Simon, S. R. / Picosecond time-resolved resonance Raman studies of hemoglobin : Implications for reactivity. In: Science. 1985 ; Vol. 229, No. 4714. pp. 661-665.
@article{676261691b134396a6fa76035f54faf8,
title = "Picosecond time-resolved resonance Raman studies of hemoglobin: Implications for reactivity",
abstract = "Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (νFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.",
author = "Findsen, {E. W.} and Friedman, {Joel M.} and Ondrias, {M. R.} and Simon, {S. R.}",
year = "1985",
language = "English (US)",
volume = "229",
pages = "661--665",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "4714",

}

TY - JOUR

T1 - Picosecond time-resolved resonance Raman studies of hemoglobin

T2 - Implications for reactivity

AU - Findsen, E. W.

AU - Friedman, Joel M.

AU - Ondrias, M. R.

AU - Simon, S. R.

PY - 1985

Y1 - 1985

N2 - Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (νFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.

AB - Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (νFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.

UR - http://www.scopus.com/inward/record.url?scp=0022412308&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022412308&partnerID=8YFLogxK

M3 - Article

VL - 229

SP - 661

EP - 665

JO - Science

JF - Science

SN - 0036-8075

IS - 4714

ER -