FeNO Structure in Distal Pocket Mutants of Myoglobin Based on Resonance Raman Spectroscopy

FeNO vibrational frequencies were investigated for a series of myoglobin mutants using isotope-edited resonance Raman spectra of 15/14NO adducts, which reveal the FeNO and NO stretching modes. The latter give rise to doublet bands, as a result of Fermi resonances with coincident porphyrin vibrations...

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Veröffentlicht in:	Biochemistry (Easton) 2003-05, Vol.42 (17), p.4896-4903
Hauptverfasser:	Coyle, Candace M, Vogel, Kathleen M, Rush, Thomas S, Kozlowski, Pawel M, Williams, Robert, Spiro, Thomas G, Dou, Yi, Ikeda-Saito, Masao, Olson, John S, Zgierski, Marek Z
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Ferric Compounds Humans Models, Molecular Mutagenesis, Site-Directed Myoglobin - chemistry Myoglobin - genetics Nitrates Protein Conformation Recombinant Proteins - chemistry Swine Whales
Online-Zugang:	Volltext
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