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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Martin, Jean-louis Negrerie, Michel Vos, Marten H. Bouzhir-sima, Latifa Liebl, Ursula |
| Description | Author Affiliation: Liebl U ( Laboratory for Optical Biosciences, Institut National de la Santé et de la Recherche Médicale U451, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7645, France.); |
| Abstract | Heme-based oxygen sensors are part of ligand-specific two-component regulatory systems, which have both a relatively low oxygen affinity and a low oxygen-binding rate. To get insight into the dynamical aspects underlying these features and the ligand specificity of the signal transduction from the heme sensor domain, we used femtosecond spectroscopy to study ligand dynamics in the heme domains of the oxygen sensors FixL from Bradyrhizobium japonicum (FixLH) and Dos from Escherichia coli (DosH). The heme coordination with different ligands and the corresponding ground-state heme spectra of FixLH are similar to myoglobin (Mb). After photodissociation, the excited-state properties and ligand-rebinding kinetics are qualitatively similar for FixLH and Mb for CO and NO as ligands. In contrast to Mb, the transient spectra of FixLH after photodissociation of ligands are distorted compared with the ground-state difference spectra, indicating differences in the heme environment with respect to the unliganded state. This distortion is particularly marked for O(2). Strikingly, heme-O(2) recombination occurs with efficiency unprecedented for heme proteins, in approximately 5 ps for approximately 90% of the dissociated O(2). For DosH-O(2), which shows 60% sequence similarity to FixLH, but where signal detection and transmission presumably are quite different, a similarly fast recombination was found with an even higher yield. Altogether these results indicate that in these sensors the heme pocket acts as a ligand-specific trap. The general implications for the functioning of heme-based ligand sensors are discussed in the light of recent studies on heme-based NO and CO sensors. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 99 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2002-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Metabolism Drosophila Proteins Eye Proteins Chemistry Hemeproteins Oxygen Bradyrhizobium Carbon Monoxide DNA Escherichia Coli Heme Kinetics Ligands Models, Biological Myoglobin Nitric Oxide Protein Binding Protein Structure, Tertiary Signal Transduction Spectrophotometry Time Factors Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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