Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

M D Roldán, H J Sears, M R Cheesman, S J Ferguson, A J Thomson, B C Berks, D J Richardson

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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 languageEnglish
Pages (from-to)28785-28790
Number of pages6
JournalJournal of Biological Chemistry
Issue number44
Publication statusPublished - 30 Oct 1998



  • Amino Acid Sequence
  • Bacteria
  • Base Sequence
  • Cytochrome c Group
  • DNA Primers
  • Electron Transport
  • Molecular Sequence Data
  • Potentiometry
  • Sequence Homology, Amino Acid
  • Spectrum Analysis
  • Journal Article
  • Research Support, Non-U.S. Gov't

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