Abstract
Mediated electrochemistry of dimethyl sulfoxide reductase from Rhodobacter capsulatus (DMSOR) which is immobilized on a bare glassy carbon (GC) electrode and a carbon nanotube (CNT)-modified GC electrode was studied using the Co complex (trans-6,13-dimethyl-1,4,8,11-tetraazacyclotetradecane-6,13-diamine)cobalt(III) ([Co(trans-diammac)]3+) as a mediator. The cyclic voltammograms of different electrodes were carried out at different substrate (DMSO) concentrations. The results demonstrated that the catalytic current was increased by employing CNT as a promoter.
Similar content being viewed by others
References
Allen PM, Hill HAO, Walton NJ. Surface modifiers for the promotion of direct electrochemistry of cytochrome c. J Electroanal Chem, 1984, 178: 69–86
Gleria KD, Hill HAO, Lowe VJ, Page DJ. Direct electrochemistry of horse-heart cytochrome c at amino acid-modified gold electrodes. J Electroanal Chem, 1986, 213: 333–338
Moghaddam AB, Ganjali MR, Dinarvand R, Saboury AA, Razavi T, Moosavi-Movahedi AA, Norouzi P. Fundamental studies of the cytochrome c immobilization by the potential cycling method on nanometer-scale nickel oxide surfaces. Biophysical Chemistry, 2007, 129: 259–268
Lu X, Zoua G., Li J. Hemoglobin entrapped within a layered spongy Co3O4 based nanocomposite featuring direct electron transfer and peroxidase activity. J Mater Chem, 2007, 17: 1427–1432
Bao SJ, Li CM, Zang JF, Cui XQ, Qiao Y, Guo J. New nanostructured TiO2 for direct electrochemistry and glucose sensor applications. Adv Funct Mater, 2008, 18: 591–599
Topoglidis E, Palomares E, Astuti Y, Green A, Cambell CJ, Durrant JR. Immobilization and electrochemistry of negatively charged proteins on modified nanocrystalline metal oxide electrodes. Electroanalysis, 2005, 17: 1035–1041
Topoglidis E, Cass AEG., O’Regan B, Durrant JR. Immobilisation and bioelectrochemistry of proteins on nanoporous TiO2 and ZnO films. J Electroanal Chem, 2001, 517: 20–27
Xu X, Tian B, Kong J, Zhang S, Liu B, Zhao D. Ordered mesoporous niobium oxide film: A novel matrix for assembling functional proteins for bioelectrochemical applications. Adv Mater, 2003, 15: 1932–1936
Dai Z, Liu S, Ju H, Chen H. Direct electron transfer and enzymatic activity of hemoglobin in a hexagonal mesoporous silica matrix. Biosens Bioelectro, 2004, 19: 861–867
Yu J, Ma J, Zhao F, Zeng B. Direct electron-transfer and electrochemical catalysis of hemoglobin immobilized on mesoporous Al2O3. Electrochimica Acta, 2007, 53: 1995–2001
Feng JJ, Xu JJ, Chen HY. Direct electron transfer and electrocatalysis of hemoglobin adsorbed on mesoporous carbon through layer-bylayer assembly. Biosens Bioelectro, 2007, 22: 1618–1624
Wang J, Li M, Shi Z, Li N, GU Z. Direct electrochemistry of cytochrome c at a glassy carbon electrode modified with single-wall carbon nanotubes. Anal Chem, 2002, 74: 1993–1997
Cai C, Chen J. Direct electron transfer of glucose oxidase promoted by carbon nanotubes. Anal Biochem, 2004, 332: 75–83
Zhao GC, Yin ZZ, Zhang L, Wei XW. Direct electrochemistry of cytochrome c on a multi-walled carbon nanotubes modified electrode and its electrocatalytic activity for the reduction of H2O2. Electrochem Comm, 2005, 7: 256–260
Zhang R, Wang X, Shiu KK. Accelerated direct electrochemistry of hemoglobin based on hemoglobin-carbon nanotube (Hb-CNT) assembly. J Colloid Interf Sci, 2007, 316: 517–522
Lu Y, Yin Y, Wu P, Cai C. Direct electrochemistry and bioelectrocatalysis of myoglobin at a carbon nanotube-modified electrode. Acta Phys-Chim Sin, 2007, 23: 5–11
Salimi A, Noorbakhsh A, Ghadermaz M. Direct electrochemistry and electrocatalytic activity of catalase incorporated onto multiwall carbon nanotubes-modiWed glassy carbon electrode. Anal Biochem, 2005, 344: 16–24
Cai C, Chen J. Direct electron transfer and bioelectrocatalysis of hemoglobin at a carbon nanotube electrode. Anal Biochem, 2004, 325: 285–292
Jiang L, McNeil CJ, Cooper JM. Direct electron transfer reactions of glucose oxidase immobilized at a self-assembled monolayer. J Chem Soc, Chem Commun, 1995, 1293-1295
Ye J, Baldwin RP. Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. Anal Chem, 1988, 60: 2263–2268
Cui X, Li CM, Zang J, Yu S. Highly sensitive lactate biosensor by engineering chitosan/PVI-Os/CNT/LOD network nanocomposite. Biosens Bioelectron, 2007, 22: 3288–3292
Aguey-Zinsou KF, Bernhardt PV, McEwan AG, Ridge JP. The first nonturnover voltammetric response from a molybdenum enzyme: direct electrochemistry of dimethylsulfoxide reductase from Rhodobacter capsulatus. J Biol Inorg Chem, 2002, 7: 879–883
Chen KI, McEwan AG, Bernhardt PV. Mediated electrochemistry of dimethyl sulfoxide reductase from Rhodobacter capsulatus. J Biol Inorg Chem, 2009, 14: 409–419
Bennett B, Benson N, McEwan AG., Bray RC. Multiple states of the molybdenum centre of dimethyl sulphoxide reductase from Rhodocacter capsulatus revealed by EPR spectroscopy. Eur J Biochem, 1994, 225: 321–331
Bernhardt PV, Lawrance GA, Hambley TW. 6,13-Diamino-6,13-dimethyl-1,4,8,11-tetra-azacyclotetradecane, L7, A new, potentially sexidentate polyamine ligand-variable coordination to cobalt (III) and crystal-structure of the complex [CO(L7)]CL2[CLO4]. J Chem Soc Dalton Trans, 1989, 1059–1065
Pearson TW, Dawson HJ, Lackey HB. Natural occurring levels of dimethyl sulfoxide in selected fruits, vegetables, grains, and beverages. J Agric Food Chem, 1981, 29: 1089–1091
Niki T, Kunugi M, Kohata K, Otsuki A. Annual monitoring of DMS-producing bacteria in Tokyo Bay, Japan, in relation to DMSP. Mar Ecol Prog Ser, 1997, 156: 17–24
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Geng, W., Zhang, L. & Bernhardt, P.V. Mediated electrochemistry of dimethyl sulfoxide reductase promoted by carbon nanotubes. Sci. China Chem. 53, 2560–2563 (2010). https://doi.org/10.1007/s11426-010-4162-1
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11426-010-4162-1