Myoglobin recombination at low temperature. Two phases revealed by Fourier transform infrared spectroscopy.

M. R. Chance, B. F. Campbell, R. Hoover, Joel M. Friedman

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The low-temperature recombination of CO with myoglobin was studied using Fourier transform infrared spectroscopy. The bound state of carbon monoxide myoglobin has two distinct conformers observed at 1926 and 1945 cm-1 with an intensity ratio of 1 to 8. The recombination of these bands after complete photolysis at 10 K followed by a temperature jump shows distinct kinetics for the two bands. Although both bands apparently follow the nonexponential kinetics originally described by Frauenfelder and co-workers (Austin, R., Beeson, K., Eisenstein, L., Frauenfelder, H., and Gunsalus, I. (1975) Biochemistry 14, 5355-5373), the 1926 cm-1 band does not appear appreciably below 70 K. In fact, after 20 min of recombination at 70 K the 1945 cm-1 band is fully recovered, while no detectable amount of the 1926 cm-1 band is present. This is the first association of a spectroscopic marker of protein substructure with reaction kinetics.

Original languageEnglish (US)
Pages (from-to)6959-6961
Number of pages3
JournalJournal of Biological Chemistry
Volume262
Issue number15
StatePublished - May 25 1987
Externally publishedYes

Fingerprint

Myoglobin
Fourier Transform Infrared Spectroscopy
Carbon Monoxide
Genetic Recombination
Biochemistry
Kinetics
Temperature
Photolysis
Reaction kinetics
Association reactions
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Myoglobin recombination at low temperature. Two phases revealed by Fourier transform infrared spectroscopy. / Chance, M. R.; Campbell, B. F.; Hoover, R.; Friedman, Joel M.

In: Journal of Biological Chemistry, Vol. 262, No. 15, 25.05.1987, p. 6959-6961.

Research output: Contribution to journalArticle

@article{66c75243d0684a14bc1bf3287f93aa48,
title = "Myoglobin recombination at low temperature. Two phases revealed by Fourier transform infrared spectroscopy.",
abstract = "The low-temperature recombination of CO with myoglobin was studied using Fourier transform infrared spectroscopy. The bound state of carbon monoxide myoglobin has two distinct conformers observed at 1926 and 1945 cm-1 with an intensity ratio of 1 to 8. The recombination of these bands after complete photolysis at 10 K followed by a temperature jump shows distinct kinetics for the two bands. Although both bands apparently follow the nonexponential kinetics originally described by Frauenfelder and co-workers (Austin, R., Beeson, K., Eisenstein, L., Frauenfelder, H., and Gunsalus, I. (1975) Biochemistry 14, 5355-5373), the 1926 cm-1 band does not appear appreciably below 70 K. In fact, after 20 min of recombination at 70 K the 1945 cm-1 band is fully recovered, while no detectable amount of the 1926 cm-1 band is present. This is the first association of a spectroscopic marker of protein substructure with reaction kinetics.",
author = "Chance, {M. R.} and Campbell, {B. F.} and R. Hoover and Friedman, {Joel M.}",
year = "1987",
month = "5",
day = "25",
language = "English (US)",
volume = "262",
pages = "6959--6961",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "15",

}

TY - JOUR

T1 - Myoglobin recombination at low temperature. Two phases revealed by Fourier transform infrared spectroscopy.

AU - Chance, M. R.

AU - Campbell, B. F.

AU - Hoover, R.

AU - Friedman, Joel M.

PY - 1987/5/25

Y1 - 1987/5/25

N2 - The low-temperature recombination of CO with myoglobin was studied using Fourier transform infrared spectroscopy. The bound state of carbon monoxide myoglobin has two distinct conformers observed at 1926 and 1945 cm-1 with an intensity ratio of 1 to 8. The recombination of these bands after complete photolysis at 10 K followed by a temperature jump shows distinct kinetics for the two bands. Although both bands apparently follow the nonexponential kinetics originally described by Frauenfelder and co-workers (Austin, R., Beeson, K., Eisenstein, L., Frauenfelder, H., and Gunsalus, I. (1975) Biochemistry 14, 5355-5373), the 1926 cm-1 band does not appear appreciably below 70 K. In fact, after 20 min of recombination at 70 K the 1945 cm-1 band is fully recovered, while no detectable amount of the 1926 cm-1 band is present. This is the first association of a spectroscopic marker of protein substructure with reaction kinetics.

AB - The low-temperature recombination of CO with myoglobin was studied using Fourier transform infrared spectroscopy. The bound state of carbon monoxide myoglobin has two distinct conformers observed at 1926 and 1945 cm-1 with an intensity ratio of 1 to 8. The recombination of these bands after complete photolysis at 10 K followed by a temperature jump shows distinct kinetics for the two bands. Although both bands apparently follow the nonexponential kinetics originally described by Frauenfelder and co-workers (Austin, R., Beeson, K., Eisenstein, L., Frauenfelder, H., and Gunsalus, I. (1975) Biochemistry 14, 5355-5373), the 1926 cm-1 band does not appear appreciably below 70 K. In fact, after 20 min of recombination at 70 K the 1945 cm-1 band is fully recovered, while no detectable amount of the 1926 cm-1 band is present. This is the first association of a spectroscopic marker of protein substructure with reaction kinetics.

UR - http://www.scopus.com/inward/record.url?scp=0023664475&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023664475&partnerID=8YFLogxK

M3 - Article

C2 - 3584103

AN - SCOPUS:0023664475

VL - 262

SP - 6959

EP - 6961

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 15

ER -