Structural and electron transfer properties of cytochromec adsorbed on graphite electrode studied by in situ tapping mode AFM

Structural and redox properties of mitochondrial cytochrome c co-sorbed with phosphate on hematite (α-Fe2O3) surfaces

“…For example, organic ions (4,4 -bipyridine is an early example [17]) have been used to prevent denaturation of adsorbed cytochrome c and to orient the heme group toward the surface to promote electron transfer [18]. Boussad et al [19] showed that phosphate can serve in a similar role for cytochrome c sorbed on graphite electrodes. Here, we investigate the co-sorption of mitochondrial cytochrome c (Cyt c) with phosphate on hematite (α-Fe 2 O 3 ) surfaces, and the effect of phosphate upon Cyt c properties while in the sorbed state, using a combination of wet chemical techniques, optical spectroscopy, atomic force microscopy, and cyclic voltammetry.…”

“…Cyt c is a peripheral c-type cytochrome responsible for transferring electrons from the mitochondrial bc 1 protein complex to cytochrome a−a 3 complex, and its complexation-induced conformation change allows it to perform its known functions [34]. Because phosphate is relatively common in nature and is known to affect Cyt c properties on other surfaces [19], its co-sorption with and effect upon Cyt c on hematite is a useful step in understanding the interaction between cytochromes and natural oxide surfaces more generally.…”

AFM and SPR studies of protein adsorption at solid/liquid interface

“…There are many studies that describe some of these techniques, which include solution depletion [14,15], gravimetry [14,16], hydrodynamic [14,17], electrical, and optical techniques [1][2][3][4]14]. The most promising techniques include ellipsometry [18], Surface…”

“…This is an extremely important development for biological applications because it allows biological samples to be imaged under conditions that are similar to the native physiological conditions. Many 3 biological samples have been examined, from DNA to proteins [3,4,25]. In addition to the biological applications, AFM has been used to examine the degradation of polymers, determine the movement of individual atoms, and fabricate metallic nanowires.…”

“…An important question that is directly related to the electron transport function of this protein is whether there is a large conformational difference between the oxidized and reduced states of cytochrome c [4][5][6][7][8][9][10]. We present a time-resolved High-Resolution Surface Plasmon…”