Spectroscopic Characterization of a Novel Multihemec-Type Cytochrome Widely Implicated in Bacterial Electron Transport

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 hem...

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Bibliographic Details
Published in:The Journal of biological chemistry 1998-11, Vol.273 (44), p.28785-28790
Main Authors: Roldán, M. Dolores, Sears, Heather J., Cheesman, Myles R., Ferguson, Stuart J., Thomson, Andrew J., Berks, Ben C., Richardson, David J.
Format: Article
Language:English
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.44.28785