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J Biol Chem, Vol. 273, Issue 44, 28785-28790, October 30, 1998

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

M. Dolores Roldán, Heather J. Sears^§, Myles R. Cheesman^¶, Stuart J. Ferguson^§, Andrew J. Thomson^¶, Ben C. Berks, and David J. Richardson

From the  School of Biological Sciences and ^¶ School of Chemical Sciences, Centre for Metalloprotein Spectroscopy and Biology, University of East Anglia, Norwich NR4 7TJ and the ^§ Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom

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.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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