Linkage of functional and structural heterogeneity in proteins

Dynamic hole burning in carboxymyoglobin

Blair F. Campbell, Mark R. Chance, Joel M. Friedman

Research output: Contribution to journalArticle

119 Citations (Scopus)

Abstract

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 substates in myoglobin rebinding. In addition, a general protocol for evaluating the relative contributions of structural relaxation and hole burning to the spectral changes accompanying ligand rebinding in hemeproteins is presented.

Original languageEnglish (US)
Pages (from-to)373-376
Number of pages4
JournalScience
Volume238
Issue number4825
StatePublished - 1987
Externally publishedYes

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Ligands
Hemeproteins
Proteins
Myoglobin
Genetic Recombination
Observation
Temperature
carboxymyoglobin

ASJC Scopus subject areas

  • General

Cite this

Linkage of functional and structural heterogeneity in proteins : Dynamic hole burning in carboxymyoglobin. / Campbell, Blair F.; Chance, Mark R.; Friedman, Joel M.

In: Science, Vol. 238, No. 4825, 1987, p. 373-376.

Research output: Contribution to journalArticle

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