The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin

Hans Frauenfelder, Benjamin H. McMahon, Robert Hamilton Austin, Kelvin Chu, John Taylor Groves

Research output: Contribution to journalArticle

295 Scopus citations

Abstract

The grail of protein science is the connection between structure and function. For myoglobin (Mb) this goal is close. Described as only a passive dioxygen storage protein in texts, we argue here that Mb is actually an allosteric enzyme that can catalyze reactions among small molecules. Studies of the structural, spectroscopic, and kinetic properties of Mb lead to a model that relates structure, energy landscape, dynamics, and function. Mb functions as a miniature chemical reactor, concentrating and orienting diatomic molecules such as NO, CO, O2, and H2O2 in highly conserved internal cavities. Reactions can be controlled because Mb exists in distinct taxonomic substates with different catalytic properties and connectivities of internal cavities.

Original languageEnglish (US)
Pages (from-to)2370-2374
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number5
DOIs
StatePublished - Feb 27 2001

All Science Journal Classification (ASJC) codes

  • General

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