Abstract
Scanning force microscopic images of cytochrome c oxidase immobilized within an electrode-supported lipid bilayer membrane are reported. These images represent the first direct evidence that the microscopic architecture of this important model system effectively mimics the microstructure proposed for the inner mitochondrial membrane. The images reveal (1) that the oxidase is present as monomers and small aggregates within the supported membrane and (2) that the oxidase constitutes ∼20% of the lipid bilayer membrane. The latter finding allows an estimation of the lower limit for the minimum turnover rate (∼0.5 electrons/s) required for the transition of the oxidase from its resting to pulsed kinetic state.
Original language | English (US) |
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Pages (from-to) | 6628-6631 |
Number of pages | 4 |
Journal | Langmuir |
Volume | 14 |
Issue number | 23 |
DOIs | |
State | Published - Nov 10 1998 |
ASJC Scopus subject areas
- Materials Science(all)
- Condensed Matter Physics
- Surfaces and Interfaces
- Spectroscopy
- Electrochemistry