Reductions by ferrocytochrome c peroxidase 4. Kinetics of yeast cytochrome c reduction at high buffer phosphate concentration

English, Ann M.; Cheung, Eddy

doi:10.1016/s0020-1693(00)85339-6

Cited by 6 publications

(6 citation statements)

References 31 publications

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“…4). This strong ionic strength dependence of Cc⅐Apaf-1 binding is consistent with the ionic strength dependence of Cc binding with its other physiological binding partners (18,19). The strong ionic strength dependence of the Cc⅐Apaf-1 interaction is also consistent with the involvement of the strongly charged surface of Cc containing the exposed heme edge.…”

Section: Resultssupporting

confidence: 78%

Cytochrome c binding to Apaf-1: The effects of dATP and ionic strength

Purring-Koch

McLendon

2000

Proc. Natl. Acad. Sci. U.S.A.

102

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In the apoptosis pathway in mammals, cytochrome c and dATP are critical cofactors in the activation of caspase 9 by Apaf-1. Until now, the detailed sequence of events in which these cofactors interact has been unclear. Here, we show through fluorescence polarization experiments that cytochrome c can bind to Apaf-1 in the absence of dATP; when dATP is added to the cytochrome c⅐Apaf-1 complex, further assembly occurs to produce the apoptosome. These findings, along with the discovery that the exposed heme edge of cytochrome c is involved in the cytochrome c⅐Apaf-1 interaction, are confirmed through enhanced chemiluminescence visualization of native PAGE gels and through acrylamide fluorescence quenching experiments. We also report here that the cytochrome c⅐Apaf-1 interaction depends highly on ionic strength, indicating that there is a strong electrostatic interaction between the two proteins.

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Section: Resultssupporting

confidence: 78%

Cytochrome c binding to Apaf-1: The effects of dATP and ionic strength

Purring-Koch

McLendon

2000

Proc. Natl. Acad. Sci. U.S.A.

102

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“…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. [17][18][19][20][21][22][23][24][25][26] Cyt has been extensively investigated not only because of the relevance of its multiple biological functions, but also as a model system for establishing the physical basis of protein electron transfer and for the development of technological devices such as sensors.…”

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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“…Therefore, when its fluorescent derivative, ZnCc, is excited with a polarized light source, most of the molecules will rotate before fluorescence occurs and the measured polarization will be small. 8 Apaf-1, on the other hand, is much larger (∼130 kDa). Thus, when ZnCc is bound to Apaf-1, the complex rotates more slowly than does ZnCc alone, leading to a higher measured polarization ratio.…”

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confidence: 97%