Linked Life Data

8312484

Source:http://linkedlifedata.com/resource/pubmed/id/8312484

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-3-23
pubmed:abstractText
In this work we report the thermal behavior (10-300 K) of the Soret band lineshape of deoxy and carbonmonoxy derivatives of Asian elephant (Elephas maximus) and horse myoglobins together with their carbon monoxide recombination kinetics after flash photolysis; the results are compared to analogous data relative to sperm whale myoglobin. The Soret band profile is modeled as a Voigt function that accounts for the coupling with high and low frequency vibrational modes, while inhomogeneous broadening is taken into account with suitable distributions of purely electronic transition frequencies. This analysis makes it possible to isolate the various contributions to the overall lineshape that; in turn, give information on structural and dynamic properties of the systems studied. The optical spectroscopy data point out sizable differences between elephant myoglobin on one hand and horse and sperm whale myoglobins on the other. These differences, more pronounced in deoxy derivatives, involve both the structure and dynamics of the heme pocket; in particular, elephant myoglobin appears to be characterized by larger anharmonic contributions to soft modes than the other two proteins. Flash photolysis data are analyzed as sums of kinetic processes with temperature-dependent fractional amplitudes, characterized by discrete pre-exponentials and either discrete or distributed activation enthalpies. In the whole temperature range investigated the behavior of elephant myoglobin appears to be more complex than that of horse and sperm whale myoglobins, which is in agreement with the increased anharmonic contributions to soft modes found in the former protein. Thus, to satisfactorily fit the time courses for CO recombination to elephant myoglobin five distinct processes are needed, only one of which is populated over the whole temperature range investigated. The remarkable convergence and complementarity between optical spectroscopy and flash photolysis data confirms the utility of combining these two experimental techniques in order to gain new and deeper insights into the functional relevance of protein fluctuations.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-1191643, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-1420893, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-1567985, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-1639188, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-1854744, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2018767, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2049528, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2231714, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2304919, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2334682, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-235432, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-2918910, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3186740, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3240362, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3293595, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3351920, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3567310, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3612808, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3663855, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3730353, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3768470, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-3860839, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-4008494, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-4012322, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-4040516, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-4415859, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-6102395, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-6296107, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-6319199, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-6643477, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7074069, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7138833, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7260037, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7265266, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7329263, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-7329277, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-8325862, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-8446624, http://linkedlifedata.com/resource/pubmed/commentcorrection/8312484-8449173
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2461-72
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Structure-dynamics-function relationships in Asian elephant (Elephas maximus) myoglobin. An optical spectroscopy and flash photolysis study on functionally important motions.
pubmed:affiliation
Istituto di Fisica, Università di Palermo, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't