The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin.
Proc Natl Acad Sci U S A
; 98(5): 2370-4, 2001 Feb 27.
Article
em En
| MEDLINE
| ID: mdl-11226246
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, O(2), and H(2)O(2) 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.
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1
Base de dados:
MEDLINE
Assunto principal:
Mioglobina
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article