Multiple conformational states in myoglobin revealed by frequency domain fluorometry.
The tryptophanyl fluorescence decays of two myoglobins, i.e., sperm whale and tuna myoglobin, have been examined in the frequency domain with an apparatus which utilizes the harmonic content of a mode-locked laser. Data analysis was performed in terms of continuous distribution of lifetime having a...
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1989
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ftcdlib:oai:escholarship.org:ark:/13030/qt5v20c26r 2023-09-05T13:23:32+02:00 Multiple conformational states in myoglobin revealed by frequency domain fluorometry. Bismuto, E Irace, G Gratton, E 1508 - 1512 1989-02-21 application/pdf https://escholarship.org/uc/item/5v20c26r unknown eScholarship, University of California qt5v20c26r https://escholarship.org/uc/item/5v20c26r CC-BY Biochemistry, vol 28, iss 4 Animals Myocardium Myoglobin Protein Conformation Spectrometry Fluorescence Tryptophan Tuna Medicinal and Biomolecular Chemistry Biochemistry and Cell Biology Medical Biochemistry and Metabolomics Biochemistry & Molecular Biology article 1989 ftcdlib 2023-08-21T18:05:14Z The tryptophanyl fluorescence decays of two myoglobins, i.e., sperm whale and tuna myoglobin, have been examined in the frequency domain with an apparatus which utilizes the harmonic content of a mode-locked laser. Data analysis was performed in terms of continuous distribution of lifetime having a Lorentzian shape. Data relative to sperm whale myoglobin, which possesses two tryptophanyl residues, i.e., Trp-A-5 and -A-12, provided a broad lifetime distribution including decay rates from a few picoseconds to about 10 ns. By contrast, the tryptophanyl lifetime distribution of tuna myoglobin, which contains only Trp-A-12, showed two well-separated and narrow Lorentzian components having centers at about 50 ps and 3.37 ns, respectively. In both cases, the chi 2 obtained from distribution analysis was lower than that provided by a fit using the sum of exponential components. The long-lived components present in the fluorescence decay of the two myoglobins do not correspond to any of those observed for the apoproteins at neutral pH. The tryptophanyl lifetime distribution of sperm whale apomyoglobin consists of two separated Lorentzian components centered at 2.25 and 5.4 ns, whereas that of tuna apomyoglobin consists of a single Lorentzian component, whose center is at 2.19 ns. Acidification of apomyoglobin to pH 3.5 produced a shift of the distribution centers toward longer lifetimes.(ABSTRACT TRUNCATED AT 250 WORDS) Article in Journal/Newspaper Sperm whale University of California: eScholarship |
institution |
Open Polar |
collection |
University of California: eScholarship |
op_collection_id |
ftcdlib |
language |
unknown |
topic |
Animals Myocardium Myoglobin Protein Conformation Spectrometry Fluorescence Tryptophan Tuna Medicinal and Biomolecular Chemistry Biochemistry and Cell Biology Medical Biochemistry and Metabolomics Biochemistry & Molecular Biology |
spellingShingle |
Animals Myocardium Myoglobin Protein Conformation Spectrometry Fluorescence Tryptophan Tuna Medicinal and Biomolecular Chemistry Biochemistry and Cell Biology Medical Biochemistry and Metabolomics Biochemistry & Molecular Biology Bismuto, E Irace, G Gratton, E Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
topic_facet |
Animals Myocardium Myoglobin Protein Conformation Spectrometry Fluorescence Tryptophan Tuna Medicinal and Biomolecular Chemistry Biochemistry and Cell Biology Medical Biochemistry and Metabolomics Biochemistry & Molecular Biology |
description |
The tryptophanyl fluorescence decays of two myoglobins, i.e., sperm whale and tuna myoglobin, have been examined in the frequency domain with an apparatus which utilizes the harmonic content of a mode-locked laser. Data analysis was performed in terms of continuous distribution of lifetime having a Lorentzian shape. Data relative to sperm whale myoglobin, which possesses two tryptophanyl residues, i.e., Trp-A-5 and -A-12, provided a broad lifetime distribution including decay rates from a few picoseconds to about 10 ns. By contrast, the tryptophanyl lifetime distribution of tuna myoglobin, which contains only Trp-A-12, showed two well-separated and narrow Lorentzian components having centers at about 50 ps and 3.37 ns, respectively. In both cases, the chi 2 obtained from distribution analysis was lower than that provided by a fit using the sum of exponential components. The long-lived components present in the fluorescence decay of the two myoglobins do not correspond to any of those observed for the apoproteins at neutral pH. The tryptophanyl lifetime distribution of sperm whale apomyoglobin consists of two separated Lorentzian components centered at 2.25 and 5.4 ns, whereas that of tuna apomyoglobin consists of a single Lorentzian component, whose center is at 2.19 ns. Acidification of apomyoglobin to pH 3.5 produced a shift of the distribution centers toward longer lifetimes.(ABSTRACT TRUNCATED AT 250 WORDS) |
format |
Article in Journal/Newspaper |
author |
Bismuto, E Irace, G Gratton, E |
author_facet |
Bismuto, E Irace, G Gratton, E |
author_sort |
Bismuto, E |
title |
Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
title_short |
Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
title_full |
Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
title_fullStr |
Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
title_full_unstemmed |
Multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
title_sort |
multiple conformational states in myoglobin revealed by frequency domain fluorometry. |
publisher |
eScholarship, University of California |
publishDate |
1989 |
url |
https://escholarship.org/uc/item/5v20c26r |
op_coverage |
1508 - 1512 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biochemistry, vol 28, iss 4 |
op_relation |
qt5v20c26r https://escholarship.org/uc/item/5v20c26r |
op_rights |
CC-BY |
_version_ |
1776204140907593728 |