Open Access. Powered by Scholars. Published by Universities.®

Physical Sciences and Mathematics Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 2 of 2

Full-Text Articles in Physical Sciences and Mathematics

Immobilization Of Cytochrome C On The Surface Of Single-Wall Carbon Nanotube And Its Direct Electron Transfer And Electrocatalysis, Ya-Jing Yin, Ya-Fen Lv, Ping Wu, Pan Du, Yan-Mao Shi, Chen-Xin Cai Aug 2006

Immobilization Of Cytochrome C On The Surface Of Single-Wall Carbon Nanotube And Its Direct Electron Transfer And Electrocatalysis, Ya-Jing Yin, Ya-Fen Lv, Ping Wu, Pan Du, Yan-Mao Shi, Chen-Xin Cai

Journal of Electrochemistry

Cytochrome c(Cyto c) was immobilized on the surface of the single-wall carbon nanotube(SWNT) by using the method of adsorption.Infrared spectroscopy indicated that the Cyto c remained in its original structure and did not undergo structural change after its immobilization on the SWNT.The direct electrochemistry of cyto c,which was adsorbed on the surface of the SWNT,was studied by cyclic voltammetry.The voltammetric results demonstrated that the SWNT had promoting effects on the direct electron transfer of Cyto c and also indicated that the immobilized Cyto c retained its bioelectrocatalytic activity to the reduction of H_(2)O_(2).This modified electrode might be used in development …


The Redox Couple Of The Cytochrome C Cyanide Complex: The Contribution Of Heme Iron Ligation To The Structural Stability, Chemical Reactivity, And Physiological Behavior Of Horse Cytochrome C, Abel Schejter, Michael D. Ryan, Erica R. Blizzard, Chongyao Zhang, Emanuel Margoliash, Benjamin A. Feinberg Jan 2006

The Redox Couple Of The Cytochrome C Cyanide Complex: The Contribution Of Heme Iron Ligation To The Structural Stability, Chemical Reactivity, And Physiological Behavior Of Horse Cytochrome C, Abel Schejter, Michael D. Ryan, Erica R. Blizzard, Chongyao Zhang, Emanuel Margoliash, Benjamin A. Feinberg

Chemistry Faculty Research and Publications

Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. In order to quantify this observation, the redox potential of the ferric/ferrous cytochrome c–cyanide redox couple was determined for the first time by cyclic voltammetry. Its E0′ was −240 mV versus SHE, equivalent to −23.2 kJ/mol. The entropy of reaction for the reduction of the cyanide complex was also determined. From a thermodynamic cycle that included this new value for the cyt c cyanide complex E0′, the binding constant of cyanide to the reduced protein was estimated to …