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NapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein. Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.

Original publication

DOI

10.1074/jbc.273.44.28785

Type

Journal article

Journal

J Biol Chem

Publication Date

30/10/1998

Volume

273

Pages

28785 - 28790

Keywords

Amino Acid Sequence, Bacteria, Base Sequence, Cytochrome c Group, DNA Primers, Electron Transport, Molecular Sequence Data, Potentiometry, Sequence Homology, Amino Acid, Spectrum Analysis