期刊
CHEMICAL SCIENCE
卷 9, 期 37, 页码 -出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8sc01716f
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资金
- Minerva (Munich) Foundation
- Israel Science Foundation
- National Natural Science Foundation of China [41630318, 41772363]
- UK Engineering and Physical Sciences Research Council [EP/M001989/1]
- Biotechnology and Biological Sciences Research Council [BB/L022176/1]
- BBSRC [BB/L022176/1] Funding Source: UKRI
- EPSRC [EP/M001946/1, EP/M001989/1] Funding Source: UKRI
Multi-heme cytochrome c (Cytc) proteins are key for transferring electrons out of cells, to enable intracellular oxidation to proceed in the absence of O-2. In these proteins most of the hemes are arranged in a linear array suggesting a facile path for electronic conduction. To test this, we studied solvent-free electron transport across two multi-heme Cytc-type proteins: MtrF (deca-heme Cytc) and STC (tetra-heme Cytc). Transport is measured across monolayers of these proteins in a solid state configuration between Au electrodes. Both proteins showed 1000x higher conductance than single heme, or heme-free proteins, but similar conductance to monolayers of conjugated organics. Conductance is found to be temperature-independent (320-80 K), suggesting tunneling as the transport mechanism. This mechanism is consistent with I-V curves modelling, results of which could be interpreted by having protein-electrode coupling as rate limiting, rather than transport within the proteins.
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