FTIR and Resonance Raman Studies of Nitric Oxide Binding to H93G Cavity Mutants of Myoglobin

Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe−NO complex. The H93G mutation eliminates the covalent attachment between the protein and the proximal ligand, allowing NO to bind H93G possibly from the proximal side of the heme rather tha...

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Veröffentlicht in:	Biochemistry (Easton) 2001-12, Vol.40 (49), p.15047-15056
Hauptverfasser:	Thomas, Melissa R, Brown, Derek, Franzen, Stefan, Boxer, Steven G
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Enzyme Inhibitors - metabolism Free Radical Scavengers - metabolism Imidazoles - metabolism Molecular Structure Mutation Myoglobin - genetics Myoglobin - metabolism Nitric Oxide - metabolism Protein Binding Spectroscopy, Fourier Transform Infrared Spectrum Analysis, Raman
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