Redox-linked conformation change and electron transfer between monoheme c-type cytochromes and oxides
| Autor: | David M. Lovelace, Nidhi Khare, Timothy S. Magnuson, Carrick M. Eggleston, Michael W. Swenson |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
biology
Cytochrome Chemistry Inorganic chemistry Oxide Hematite Electrochemistry biology.organism_classification Redox Electron transfer Crystallography chemistry.chemical_compound Geochemistry and Petrology visual_art visual_art.visual_art_medium biology.protein medicine Ferric Acidiphilium cryptum medicine.drug |
| Zdroj: | Geochimica et Cosmochimica Acta. 70:4332-4342 |
| ISSN: | 0016-7037 |
| DOI: | 10.1016/j.gca.2006.06.1561 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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