Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy

Haruto Ishikawa, Ilya J. Finkelstein, Seongheun Kim, Kyungwon Kwak, Jean K. Chung, Keisuke Wakasugi, Aaron M. Massari, Michael D. Fayer

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Neuroglobin (Ngb), a protein in the globin family, is found in vertebrate brains. It binds oxygen reversibly. Compared with myoglobin (Mb), the amino acid sequence has limited similarity, but key residues around the heme and the classical globin fold are conserved in Ngb. The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N 3 (distal histidine in the pocket) and N 0 (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. The Mb mutants mimic the heme pocket structures of the corresponding Ngb conformers. The equilibrium protein dynamics for the CO adduct of Ngb are investigated by using ultrafast 2D-IR vibrational echo spectroscopy by observing the CO vibration's spectral diffusion (2D-IR spectra time dependence) and comparing the results with those for the Mb mutants. Although the heme pocket structure and the CO FTIR peak positions of Ngb are similar to those of the mutant Mb proteins, the 2D-IR results demonstrate that the fast structural fluctuations of Ngb are significantly slower than those of the mutant Mbs. The results may also provide some insights into the nature of the energy landscape in the vicinity of the folded protein free energy minimum.

Original languageEnglish
Pages (from-to)16116-16121
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number41
DOIs
Publication statusPublished - 2007 Oct 9
Externally publishedYes

Fingerprint

Spectrum Analysis
Myoglobin
Carbon Monoxide
Heme
Globins
Histidine
Proteins
Fourier Transform Infrared Spectroscopy
Mutant Proteins
Vibration
neuroglobin
Vertebrates
Amino Acid Sequence
Oxygen
Brain

Keywords

  • Energy landscape
  • Myoglobin mutants
  • Protein dynamics

ASJC Scopus subject areas

  • General

Cite this

Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy. / Ishikawa, Haruto; Finkelstein, Ilya J.; Kim, Seongheun; Kwak, Kyungwon; Chung, Jean K.; Wakasugi, Keisuke; Massari, Aaron M.; Fayer, Michael D.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, No. 41, 09.10.2007, p. 16116-16121.

Research output: Contribution to journalArticle

Ishikawa, Haruto ; Finkelstein, Ilya J. ; Kim, Seongheun ; Kwak, Kyungwon ; Chung, Jean K. ; Wakasugi, Keisuke ; Massari, Aaron M. ; Fayer, Michael D. / Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy. In: Proceedings of the National Academy of Sciences of the United States of America. 2007 ; Vol. 104, No. 41. pp. 16116-16121.
@article{16cd0426c812400bbb1c77b9a68ffc91,
title = "Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy",
abstract = "Neuroglobin (Ngb), a protein in the globin family, is found in vertebrate brains. It binds oxygen reversibly. Compared with myoglobin (Mb), the amino acid sequence has limited similarity, but key residues around the heme and the classical globin fold are conserved in Ngb. The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N 3 (distal histidine in the pocket) and N 0 (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. The Mb mutants mimic the heme pocket structures of the corresponding Ngb conformers. The equilibrium protein dynamics for the CO adduct of Ngb are investigated by using ultrafast 2D-IR vibrational echo spectroscopy by observing the CO vibration's spectral diffusion (2D-IR spectra time dependence) and comparing the results with those for the Mb mutants. Although the heme pocket structure and the CO FTIR peak positions of Ngb are similar to those of the mutant Mb proteins, the 2D-IR results demonstrate that the fast structural fluctuations of Ngb are significantly slower than those of the mutant Mbs. The results may also provide some insights into the nature of the energy landscape in the vicinity of the folded protein free energy minimum.",
keywords = "Energy landscape, Myoglobin mutants, Protein dynamics",
author = "Haruto Ishikawa and Finkelstein, {Ilya J.} and Seongheun Kim and Kyungwon Kwak and Chung, {Jean K.} and Keisuke Wakasugi and Massari, {Aaron M.} and Fayer, {Michael D.}",
year = "2007",
month = "10",
day = "9",
doi = "10.1073/pnas.0707718104",
language = "English",
volume = "104",
pages = "16116--16121",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "41",

}

TY - JOUR

T1 - Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy

AU - Ishikawa, Haruto

AU - Finkelstein, Ilya J.

AU - Kim, Seongheun

AU - Kwak, Kyungwon

AU - Chung, Jean K.

AU - Wakasugi, Keisuke

AU - Massari, Aaron M.

AU - Fayer, Michael D.

PY - 2007/10/9

Y1 - 2007/10/9

N2 - Neuroglobin (Ngb), a protein in the globin family, is found in vertebrate brains. It binds oxygen reversibly. Compared with myoglobin (Mb), the amino acid sequence has limited similarity, but key residues around the heme and the classical globin fold are conserved in Ngb. The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N 3 (distal histidine in the pocket) and N 0 (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. The Mb mutants mimic the heme pocket structures of the corresponding Ngb conformers. The equilibrium protein dynamics for the CO adduct of Ngb are investigated by using ultrafast 2D-IR vibrational echo spectroscopy by observing the CO vibration's spectral diffusion (2D-IR spectra time dependence) and comparing the results with those for the Mb mutants. Although the heme pocket structure and the CO FTIR peak positions of Ngb are similar to those of the mutant Mb proteins, the 2D-IR results demonstrate that the fast structural fluctuations of Ngb are significantly slower than those of the mutant Mbs. The results may also provide some insights into the nature of the energy landscape in the vicinity of the folded protein free energy minimum.

AB - Neuroglobin (Ngb), a protein in the globin family, is found in vertebrate brains. It binds oxygen reversibly. Compared with myoglobin (Mb), the amino acid sequence has limited similarity, but key residues around the heme and the classical globin fold are conserved in Ngb. The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N 3 (distal histidine in the pocket) and N 0 (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. The Mb mutants mimic the heme pocket structures of the corresponding Ngb conformers. The equilibrium protein dynamics for the CO adduct of Ngb are investigated by using ultrafast 2D-IR vibrational echo spectroscopy by observing the CO vibration's spectral diffusion (2D-IR spectra time dependence) and comparing the results with those for the Mb mutants. Although the heme pocket structure and the CO FTIR peak positions of Ngb are similar to those of the mutant Mb proteins, the 2D-IR results demonstrate that the fast structural fluctuations of Ngb are significantly slower than those of the mutant Mbs. The results may also provide some insights into the nature of the energy landscape in the vicinity of the folded protein free energy minimum.

KW - Energy landscape

KW - Myoglobin mutants

KW - Protein dynamics

UR - http://www.scopus.com/inward/record.url?scp=36049026900&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36049026900&partnerID=8YFLogxK

U2 - 10.1073/pnas.0707718104

DO - 10.1073/pnas.0707718104

M3 - Article

C2 - 17916624

AN - SCOPUS:36049026900

VL - 104

SP - 16116

EP - 16121

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 41

ER -