Heme Binding in Gas-Phase Holo-Myoglobin Cations: Distal Becomes Proximal?

His64 and His93 are the two well-known sites of heme binding in water-dissolved holo-myoglobin, with His93 being a proximal, strongly binding partner, while the distal His64 weakly coordinates to the heme through a small-molecule ligand, e.g., water or O 2 . The heme bonding scheme in a water-free e...

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Veröffentlicht in:	Journal of the American Society for Mass Spectrometry 2011-10, Vol.22 (10), p.1763-1770, Article s13361-011-0182-0
Hauptverfasser:	Enyenihi, Atim A., Yang, Hongqian, Ytterberg, A. Jimmy, Lyutvinskiy, Yaroslav, Zubarev, Roman A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical Chemistry Analytical, structural and metabolic biochemistry Animals Binding Binding Sites Bioinformatics Biological and medical sciences Biotechnology Cations - chemistry Chemical bonds Chemistry Chemistry and Materials Science Electron transfer Fundamental and applied biological sciences. Psychology General aspects, investigation methods Heme - chemistry Heme - metabolism Histidine Histidine - chemistry Horses Mass spectrometry Models, Molecular Molecular Sequence Data Myoglobin - chemistry Myoglobin - metabolism Myoglobins Organic Chemistry Protein Binding Proteins Proteomics Protonation Research Article Spectrometry, Mass, Electrospray Ionization
Online-Zugang:	Volltext
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