Publication Date:
1987-10-16
Description:
Inhomogeneous broadening of the 760-nanometer photoproduct band of carboxymyoglobin at cryogenic temperatures has been demonstrated with a dynamic hole burning technique. Line-shape changes and frequency shifts in this spectral band are generated by ligand recombination and are shown not to be the result of structural relaxation below 60 K. The observation of dynamic hole burning exposes the relation between the structural disorder responsible for the inhomogeneous broadening and the well-known distributed ligand rebinding kinetics. The findings provide direct evidence for the functional relevance of conformational substrates in myoglobin rebinding. In addition, a general protocol for evaluating the relative contributions of structural relaxation and hole burning to the spectral changes accompanying rebinding in hemeproteins is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Campbell, B F -- Chance, M R -- Friedman, J M -- HL-18708/HL/NHLBI NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉AT&T Bell Laboratories, Murray Hill, NJ 07974.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659921" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Carbon Monoxide/metabolism
;
Kinetics
;
Myoglobin/*metabolism
;
Photochemistry
;
Protein Binding
;
Protein Conformation
;
Spectrophotometry
;
Spectrophotometry, Infrared
;
Temperature
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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