Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Mechanisms of Electron Transfer in Two Decaheme Cytochromes from a Metal-Reducing Bacterium

Journal Article · · Journal of Physical Chemistry B, 111(44):12857-12864
DOI:https://doi.org/10.1021/jp0718698· OSTI ID:920535

Single-molecule current-voltage (I–V) spectra were collected using a scanning tunneling microscope for two decaheme c-type cytochromes, OmcA and MtrC, which are outer-membrane proteins from the dissimilatory metal-reducing bacterium Shewanella oneidensis. Although the two cytochromes are similar in heme count, charge-carrying amino-acid content, and molecular mass, their I–V spectra are significantly different. The I–V spectra for OmcA show smoothly varying symmetric exponential behavior. These spectra are well fit by a coherent tunneling model that is based on a simple square barrier description of the tunneling junction. In contrast, the I–V spectra for MtrC have pronounced breaks in slope in the positive tip bias range. Two large peaks in the normalized differential conductance spectra of MtrC were fit to a tunneling model that accounts for the possibility of transient population of empty states stabilized by vibrational relaxation. Reorganization energies deduced for the two features are similar to those normally assigned to metal centers in other metalloproteins. Work function measurements of the cytochrome films were used to convert the energies of these two spectral features to the normal hydrogen electrode scale for comparison with the midpoint potential measured using protein film voltammetry, which showed good correspondence. We conclude that MtrC mediates tunneling current by heme orbital participation. The difference in tunneling behavior between OmcA and MtrC suggests distinct physiological functions for the two cytochromes; in contrast to OmcA, MtrC appears to be tuned to a specific operating potential.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
920535
Report Number(s):
PNNL-SA-54180
Journal Information:
Journal of Physical Chemistry B, 111(44):12857-12864, Journal Name: Journal of Physical Chemistry B, 111(44):12857-12864 Journal Issue: 44 Vol. 111
Country of Publication:
United States
Language:
English

Similar Records

Electron tunneling properties of outer-membrane decaheme cytochromes from Shewanella oneidensis
Journal Article · Wed Jan 31 23:00:00 EST 2007 · Geochimica et Cosmochimica Acta · OSTI ID:902041

Isolation of a High-Affinity Functional Protein Complex between OmcA and MtrC: Two Outer Membrane Decaheme c-type Cytochromes of Shewanella oneidensis MR-1
Journal Article · Sat Jul 01 00:00:00 EDT 2006 · Journal of Bacteriology, 188(13):4705-4714 · OSTI ID:885441

Characterization of Shewanella oneidensis MtrC: a cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors
Journal Article · Tue Sep 04 00:00:00 EDT 2007 · Journal of Biological Inorganic Chemistry, 12(7):1083-1094 · OSTI ID:918455