Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 14, Issue 20, Pages 7411-7419Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2cp23568d
Keywords
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Funding
- European Research Council [202706]
- Science and Technology Facilities Council
- European Research Council (ERC) [202706] Funding Source: European Research Council (ERC)
- Biotechnology and Biological Sciences Research Council [1412459] Funding Source: researchfish
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The ultrafast equilibrium fluctuations of the Fe-III-NO complex of a single point mutation of Myoglobin (H64Q) have been studied using Fourier Transform 2D-IR spectroscopy. Comparison with data from wild type Myoglobin (wt-Mb) shows the presence of two conformational substates of the mutant haem pocket where only one exists in the wild type form. One of the substates of the mutant exhibits an almost identical NO stretching frequency and spectral diffusion dynamics to wt-Mb while the other is distinctly different in both respects. The remarkably contrasting dynamics are largely attributable to interactions between the NO ligand and a nearby distal side chain which provides a basis for understanding the roles of these side chains in other ferric haem proteins.
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