Flavohemoglobin, a Globin with a Peroxidase-like Catalytic Site

Biochemical studies of flavohemoglobin (Hmp) from Escherichia coli suggest that instead of aerobic oxygen delivery, a dioxygenase converts NO to NO3− and anaerobically, an NO reductase converts NO to N2O. To investigate the structural features underlying the chemical reactivity of Hmp, we have measu...

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Veröffentlicht in:	The Journal of biological chemistry 2001-03, Vol.276 (10), p.7272-7277
Hauptverfasser:	Mukai, Masahiro, Mills, Catherine E., Poole, Robert K., Yeh, Syun-Ru
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Binding Sites Carbon - chemistry Catalytic Domain Cloning, Molecular Dihydropteridine Reductase Escherichia coli Escherichia coli Proteins flavohemoglobin Hemeproteins - chemistry Hemeproteins - genetics Hydrogen-Ion Concentration Iron - metabolism Ligands Models, Chemical Models, Molecular NADH, NADPH Oxidoreductases Nitric Oxide - metabolism Oxidoreductases - metabolism Oxygen - chemistry Oxygen - metabolism Oxygenases Peroxidase - chemistry Protein Conformation Spectrum Analysis, Raman
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