Characterization of cytochrome c folding intermediates induced by sucrose and phosphate

Ahluwalia, Unnati; Prakash, Chetan; Agrawal, Rakhi; Deep, Shashank

doi:10.1016/j.ijbiomac.2011.07.010

Cited by 2 publications

(1 citation statement)

References 28 publications

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“…1 Moreover, it has been shown that Cyt is able to bind specifically a number of anions, including chloride, phosphate, ATP, ADP, nitrate, sulfate, perchlorate, citrate, and oxalate. Ion binding has been reported to affect or modulate properties and processes of Cyt, such as reduction potential, 6,11,[13][14][15] protein folding, 7,9 the so-called alkaline transition, 8 heat stability, 12 electrophoretic and chromatographic behavior, 16,17 binding to Apaf-1, 27,28 and electron transfer kinetics with natural and artificial redox partners. 1,26,[29][30][31][32][33][34] The binding domains for some of these anions have been studied using NMR and computational methods for both the native and chemically modified protein.…”

Section: Introductionmentioning

confidence: 99%

Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study

Capdevila

Marmisollé

Williams

et al. 2013

Phys. Chem. Chem. Phys.

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The study of proteins immobilized on biomimetic or biocompatible electrodes represents an active field of research as it pursues both fundamental and technological interests. In this context, adsorption and redox properties of cytochrome c (Cyt) on different electrode surfaces have been extensively reported, although in some cases with contradictory results. Here we report a SERR spectroelectrochemical study of the adsorption and electron transfer behaviour of the basic protein Cyt on electrodes coated with amino-terminated monolayers. The obtained results show that inorganic phosphate (Pi) and ATP anions are able to mediate high affinity binding of the protein with preservation of the native structure and rendering an average orientation that guarantees efficient pathways for direct electron transfer. These findings aid the design of Cyt-based bioelectronic devices and understanding the modulation by Pi and ATP of physiological functions of Cyt.

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