schliessen

Filtern

 

Bibliotheken

Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.

Encapsulation of hemoglobin (Hb) in silica gel preserves structure and function but greatly slows protein motion, thereby providing access to intermediates along the allosteric pathway that are inaccessible in solution. Resonance Raman (RR) spectroscopy with visible and ultraviolet laser excitation... Full description

Journal Title: Journal of the American Chemical Society February 22, 2012, Vol.134(7), pp.3461-3471
Main Author: Jones, Eric M
Other Authors: Balakrishnan, Gurusamy , Spiro, Thomas G
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja210126j
Link: http://search.proquest.com/docview/923192582/?pq-origsite=primo
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest923192582
title: Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
format: Article
creator:
  • Jones, Eric M
  • Balakrishnan, Gurusamy
  • Spiro, Thomas G
subjects:
  • Carbon Monoxide–Metabolism
  • Heme–Chemistry
  • Hemoglobin A–Metabolism
  • Humans–Chemistry
  • Immobilized Proteins–Metabolism
  • Models, Molecular–Chemistry
  • Protein Structure, Tertiary–Metabolism
  • Spectrum Analysis, Raman–Methods
  • Immobilized Proteins
  • Heme
  • Carbon Monoxide
  • Hemoglobin A
ispartof: Journal of the American Chemical Society, February 22, 2012, Vol.134(7), pp.3461-3471
description: Encapsulation of hemoglobin (Hb) in silica gel preserves structure and function but greatly slows protein motion, thereby providing access to intermediates along the allosteric pathway that are inaccessible in solution. Resonance Raman (RR) spectroscopy with visible and ultraviolet laser excitation provides probes of heme reactivity and of key tertiary and quaternary contacts. These probes were monitored in gels after deoxygenation of oxyHb and after CO binding to deoxyHb, which initiate conformational change in the R-T and T-R directions, respectively. The spectra establish that quaternary structure change in the gel takes a week or more but that the evolution of heme reactivity, as monitored by the Fe-histidine stretching vibration, ν(FeHis), is completed within two days, and is therefore uncoupled from the quaternary structure. Within each quaternary structure, the evolving ν(FeHis) frequencies span the full range of values between those previously associated with the high- and low-affinity end states, R and T. This result supports the tertiary two-state (TTS) model, in which the Hb subunits can adopt high- and low-affinity tertiary structures, r and t, within each quaternary state. The spectra also reveal different tertiary pathways, involving the breaking and reformation of E and F interhelical contacts in the R-T direction but not the T-R direction. In the latter, tertiary motions are restricted by the T quaternary contacts.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja210126j
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


@attributes
ID119048524
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid923192582
sourceidproquest
recordidTN_proquest923192582
sourcesystemOther
pqid923192582
galeid286852265
display
typearticle
titleHeme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
creatorJones, Eric M ; Balakrishnan, Gurusamy ; Spiro, Thomas G
contributorJones, Eric M (correspondence author) ; Jones, Eric M (record owner)
ispartofJournal of the American Chemical Society, February 22, 2012, Vol.134(7), pp.3461-3471
identifier
subjectCarbon Monoxide–Metabolism ; Heme–Chemistry ; Hemoglobin A–Metabolism ; Humans–Chemistry ; Immobilized Proteins–Metabolism ; Models, Molecular–Chemistry ; Protein Structure, Tertiary–Metabolism ; Spectrum Analysis, Raman–Methods ; Immobilized Proteins ; Heme ; Carbon Monoxide ; Hemoglobin A
languageeng
source
descriptionEncapsulation of hemoglobin (Hb) in silica gel preserves structure and function but greatly slows protein motion, thereby providing access to intermediates along the allosteric pathway that are inaccessible in solution. Resonance Raman (RR) spectroscopy with visible and ultraviolet laser excitation provides probes of heme reactivity and of key tertiary and quaternary contacts. These probes were monitored in gels after deoxygenation of oxyHb and after CO binding to deoxyHb, which initiate conformational change in the R-T and T-R directions, respectively. The spectra establish that quaternary structure change in the gel takes a week or more but that the evolution of heme reactivity, as monitored by the Fe-histidine stretching vibration, ν(FeHis), is completed within two days, and is therefore uncoupled from the quaternary structure. Within each quaternary structure, the evolving ν(FeHis) frequencies span the full range of values between those previously associated with the high- and low-affinity end states, R and T. This result supports the tertiary two-state (TTS) model, in which the Hb subunits can adopt high- and low-affinity tertiary structures, r and t, within each quaternary state. The spectra also reveal different tertiary pathways, involving the breaking and reformation of E and F interhelical contacts in the R-T direction but not the T-R direction. In the latter, tertiary motions are restricted by the T quaternary contacts.
version3
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
backlink$$Uhttp://search.proquest.com/docview/923192582/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontrib
0Jones, Eric M
1Balakrishnan, Gurusamy
2Spiro, Thomas G
titleHeme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
subject
0Carbon Monoxide–Metabolism
1Heme–Chemistry
2Hemoglobin A–Metabolism
3Humans–Chemistry
4Immobilized Proteins–Metabolism
5Models, Molecular–Chemistry
6Protein Structure, Tertiary–Metabolism
7Spectrum Analysis, Raman–Methods
8Immobilized Proteins
9Heme
10Carbon Monoxide
11Hemoglobin A
general
0English
11520-5126
210.1021/ja210126j
3MEDLINE (ProQuest)
4ProQuest Biological Science Collection
5ProQuest Natural Science Collection
6ProQuest SciTech Collection
7Biological Science Database
8Natural Science Collection
9SciTech Premium Collection
10Health Research Premium Collection
11Health Research Premium Collection (Alumni edition)
sourceidproquest
recordidproquest923192582
issn
015205126
11520-5126
rsrctypearticle
creationdate2012
addtitleJournal of the American Chemical Society
searchscope
01007527
11007944
210000004
310000038
410000050
510000120
610000159
710000238
810000253
910000260
1010000270
1110000271
1210000302
13proquest
scope
01007527
11007944
210000004
310000038
410000050
510000120
610000159
710000238
810000253
910000260
1010000270
1110000271
1210000302
13proquest
lsr43
01007527false
11007944false
210000004false
310000038false
410000050false
510000120false
610000159false
710000238false
810000253false
910000260false
1010000270false
1110000271false
1210000302false
contributorJones, Eric M
startdate20120222
enddate20120222
citationpf 3461 pt 3471 vol 134 issue 7
lsr30VSR-Enriched:[galeid, description, pqid]
sort
titleHeme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
authorJones, Eric M ; Balakrishnan, Gurusamy ; Spiro, Thomas G
creationdate20120222
lso0120120222
facets
frbrgroupid8893894307917691071
frbrtype5
newrecords20181218
languageeng
creationdate2012
topic
0Carbon Monoxide–Metabolism
1Heme–Chemistry
2Hemoglobin A–Metabolism
3Humans–Chemistry
4Immobilized Proteins–Metabolism
5Models, Molecular–Chemistry
6Protein Structure, Tertiary–Metabolism
7Spectrum Analysis, Raman–Methods
8Immobilized Proteins
9Heme
10Carbon Monoxide
11Hemoglobin A
collection
0MEDLINE (ProQuest)
1ProQuest Biological Science Collection
2ProQuest Natural Science Collection
3ProQuest SciTech Collection
4Biological Science Database
5Natural Science Collection
6SciTech Premium Collection
7Health Research Premium Collection
8Health Research Premium Collection (Alumni edition)
prefilterarticles
rsrctypearticles
creatorcontrib
0Jones, Eric M
1Balakrishnan, Gurusamy
2Spiro, Thomas G
jtitleJournal of the American Chemical Society
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextno_fulltext
addata
aulast
0Jones
1Balakrishnan
2Spiro
aufirst
0Eric M
1Gurusamy
2Thomas G
au
0Jones, Eric M
1Balakrishnan, Gurusamy
2Spiro, Thomas G
addauJones, Eric M
atitleHeme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
jtitleJournal of the American Chemical Society
risdate20120222
volume134
issue7
spage3461
epage3471
pages3461-3471
eissn1520-5126
formatjournal
genrearticle
ristypeJOUR
doi10.1021/ja210126j
urlhttp://search.proquest.com/docview/923192582/
date2012-02-22