Structure and Spectroscopy of the Periplasmic Cytochrome c Nitrite Reductase from Escherichia coli
作者： Vicki A Bamford , Hayley C Angove , Harriet E Seward , Andrew J Thomson , Jeffrey A Cole
DOI: 10.1021/BI015765D
关键词: Electron paramagnetic resonance 、 Escherichia coli 、 Cytochrome 、 Stereochemistry 、 Redox 、 Photochemistry 、 Cytochrome c nitrite reductase 、 Oxidoreductase 、 Chemistry 、 Heme 、 Periplasmic space
摘要: The crystal structure and spectroscopic properties of the periplasmic penta-heme cytochrome c nitrite reductase (NrfA) Escherichia coli are presented. is first for a member NrfA subgroup that utilize soluble cytochrome, NrfB, as redox partner. Comparison to structures Wolinella succinogenes Sulfospirillum deleyianum NrfA, which accept electrons from membrane-anchored tetra-heme (NrfH), reveals notable differences in protein surface around heme 2, may be docking site shows four hemes (hemes 2−5) have bis-histidine axial heme-Fe ligation. catalytic (heme 1) has lysine distal ligand an oxygen atom proximal ligand. Analysis solution by magnetic circular dichroism (MCD) suggested arose water. Electron paramagnetic resonance (EPR) spectra were collected electrochemically poised samples. Broad perpendicular m...
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