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Redox-linked conformation change and electron transfer between monoheme c-type cytochromes and oxides

Journal Article · · Geochimica et Cosmochimica Acta, 70(17):4332-4342
Electron transfer between redox active proteins and mineral oxides is important in a variety of natural as well as technological processes, including electron transfer from dissimilatory metal-reducing bacteria to minerals. One of the pathways that could trigger electron transfer between proteins and minerals is redox-linked conformation change. We present electrochemical evidence that mitochondrial cytochrome c (Mcc) undergoes significant conformation change upon interaction with hematite and indium-tin oxide (ITO) surfaces. The apparent adsorption-induced conformation change causes the protein to become more reducing, which makes it able to transfer electrons to the hematite conduction band. Although Mcc is not a protein thought to be involved in interaction with mineral surfaces, it shares (or can be conformed so as to share) some characteristics with multiheme outer-membrane cytochromes thought to be involved in the transfer of electrons from dissimilatory iron-reducing bacteria to ferric minerals during respiration. We present evidence that a 10.1 kDa monohoeme cytochrome isolated and purified from Acidiphilium cryptum, with properties similar to those of Mcc, also undergoes conformation change as a result of interaction with hematite surfaces.
Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
944781
Report Number(s):
PNNL-SA-61710; 13890; KP1504020
Journal Information:
Geochimica et Cosmochimica Acta, 70(17):4332-4342, Journal Name: Geochimica et Cosmochimica Acta, 70(17):4332-4342 Journal Issue: 17 Vol. 70; ISSN GCACAK; ISSN 0016-7037
Country of Publication:
United States
Language:
English