Folding of Deoxymyoglobin Triggered by Electron Transfer

The met and deoxy forms of sperm whale myoglobin (Mb) can be unfolded by guanidine hydrochloride (GuHCl). Electronic absorption and circular dichroism spectroscopic measurements show that folded deoxyMb is more stable than the folded met protein. Laser excitation of NADH generates species that rapid...

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Published in:The Journal of Physical Chemistry A
Main Authors: Wittung-Stafshede, Pernilla, Malmström, Bo G., Winkler, Jay R., Gray, Harry B.
Format: Article in Journal/Newspaper
Language:unknown
Published: American Chemical Society 1998
Subjects:
Sperm whale
Online Access:https://authors.library.caltech.edu/85293/
https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459
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spelling ftcaltechauth:oai:authors.library.caltech.edu:85293 2023-05-15T18:26:39+02:00 Folding of Deoxymyoglobin Triggered by Electron Transfer Wittung-Stafshede, Pernilla Malmström, Bo G. Winkler, Jay R. Gray, Harry B. 1998-07-09 https://authors.library.caltech.edu/85293/ https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459 unknown American Chemical Society Wittung-Stafshede, Pernilla and Malmström, Bo G. and Winkler, Jay R. and Gray, Harry B. (1998) Folding of Deoxymyoglobin Triggered by Electron Transfer. Journal of Physical Chemistry A, 102 (28). pp. 5599-5601. ISSN 1089-5639. doi:10.1021/jp9802228. https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459 <https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459> Article PeerReviewed 1998 ftcaltechauth https://doi.org/10.1021/jp9802228 2021-11-18T18:45:14Z The met and deoxy forms of sperm whale myoglobin (Mb) can be unfolded by guanidine hydrochloride (GuHCl). Electronic absorption and circular dichroism spectroscopic measurements show that folded deoxyMb is more stable than the folded met protein. Laser excitation of NADH generates species that rapidly reduce unfolded metMb, triggering the formation of folded deoxyMb in less than 10 ms (pH 7.0, 2.5 to 3 M GuHCl, 20 °C). At comparable reaction driving forces (∼10 kJ/mol), deoxyMb folds much faster than reduced cytochrome c. Article in Journal/Newspaper Sperm whale Caltech Authors (California Institute of Technology) The Journal of Physical Chemistry A 102 28 5599 5601
institution Open Polar
collection Caltech Authors (California Institute of Technology)
op_collection_id ftcaltechauth
language unknown
description The met and deoxy forms of sperm whale myoglobin (Mb) can be unfolded by guanidine hydrochloride (GuHCl). Electronic absorption and circular dichroism spectroscopic measurements show that folded deoxyMb is more stable than the folded met protein. Laser excitation of NADH generates species that rapidly reduce unfolded metMb, triggering the formation of folded deoxyMb in less than 10 ms (pH 7.0, 2.5 to 3 M GuHCl, 20 °C). At comparable reaction driving forces (∼10 kJ/mol), deoxyMb folds much faster than reduced cytochrome c.
format Article in Journal/Newspaper
author Wittung-Stafshede, Pernilla
Malmström, Bo G.
Winkler, Jay R.
Gray, Harry B.
spellingShingle Wittung-Stafshede, Pernilla
Malmström, Bo G.
Winkler, Jay R.
Gray, Harry B.
Folding of Deoxymyoglobin Triggered by Electron Transfer
author_facet Wittung-Stafshede, Pernilla
Malmström, Bo G.
Winkler, Jay R.
Gray, Harry B.
author_sort Wittung-Stafshede, Pernilla
title Folding of Deoxymyoglobin Triggered by Electron Transfer
title_short Folding of Deoxymyoglobin Triggered by Electron Transfer
title_full Folding of Deoxymyoglobin Triggered by Electron Transfer
title_fullStr Folding of Deoxymyoglobin Triggered by Electron Transfer
title_full_unstemmed Folding of Deoxymyoglobin Triggered by Electron Transfer
title_sort folding of deoxymyoglobin triggered by electron transfer
publisher American Chemical Society
publishDate 1998
url https://authors.library.caltech.edu/85293/
https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459
genre Sperm whale
genre_facet Sperm whale
op_relation Wittung-Stafshede, Pernilla and Malmström, Bo G. and Winkler, Jay R. and Gray, Harry B. (1998) Folding of Deoxymyoglobin Triggered by Electron Transfer. Journal of Physical Chemistry A, 102 (28). pp. 5599-5601. ISSN 1089-5639. doi:10.1021/jp9802228. https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459 <https://resolver.caltech.edu/CaltechAUTHORS:20180313-160333459>
op_doi https://doi.org/10.1021/jp9802228
container_title The Journal of Physical Chemistry A
container_volume 102
container_issue 28
container_start_page 5599
op_container_end_page 5601
_version_ 1766208621756022784

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