Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 12, Pages 3692-3696Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201410247
Keywords
charge resonance; electronic structure; heme proteins; high-valence iron; near-infrared spectroscopy
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Funding
- National Institutes of Health [R01GM108988]
- Georgia Research Alliance Distinguished Scholar Program
- William M. Suttles doctoral research fellowship from Georgia State University
- Georgia State University
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM108988] Funding Source: NIH RePORTER
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The biosynthesis of tryptophan tryptophylquinone, a protein-derived cofactor, involves a long-range reaction mediated by a bis-Fe-IV intermediate of a diheme enzyme, MauG. Recently, a unique charge-resonance (CR) phenomenon was discovered in this intermediate, and a biological, long-distance CR model was proposed. This model suggests that the chemical nature of the bis-Fe-IV species is not as simple as it appears; rather, it is composed of a collection of resonance structures in a dynamic equilibrium. Here, we experimentally evaluated the proposed CR model by introducing small molecules to, and measuring the temperature dependence of, bis-Fe-IV MauG. Spectroscopic evidence was presented to demonstrate that the selected compounds increase the decay rate of the bis-Fe-IV species by disrupting the equilibrium of the resonance structures that constitutes the proposed CR model. The results support this new CR model and bring a fresh concept to the classical CR theory.
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