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Redox-Linked Conformation Change and Electron Transfer Between Monoheme C-Type Cytochromes and Oxides
Khare, N. Lovelace, D. M. Eggleston, Carrick Swenson, M. Magnuson, T. S.
Khare, N.
Lovelace, D. M.
Eggleston, Carrick
Swenson, M.
Magnuson, T. S.
Abstract
Description
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 cytochrorne c (Mee) undergoes significant conformation change upon interaction with hematite and indiurn-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 cytochrorne 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.
Date
2006-09-01
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University of Wyoming. Libraries
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Keywords
Geology