@article{citeulike:498925,
        title = {Redox mediation and photomechanical oscillations involving photosensitive cyclometalated Ru(II) complexes, glucose oxidase, and peroxidase.},
        address = {Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. ryabov@andrew.cmu.edu},
        author = {A. D. Ryabov and V. S. Kurova and E. V. Ivanova and R. Le Lagadec and L. Alexandrova},
        journal = {Anal Chem},
        month = {February},
        number = 4,
        pages = {1132--1139},
        volume = 77,
        year = 2005,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=15858996},
        id = {498925},
	issn = {0003-2700},
	priority = {2},
	comment = {ryabov@andrew.cmu.edu},
	doi = {10.1021/ac048743g},
	abstract = {Intact photosensitive cyclometalated RuII derivatives of 2-phenylpyridine or N,N-dimethylbenzylamine cis-[Ru-(C approximately N)(LL)X2]PF6 [C approximately N = o-C6H4-py or o-C6H4CH2NMe2; LL = 1,10-phenanththroline (phen), 2,2'-bipyridine (bpy), or 4,4'-Me2-2,2'-bipyridine (Me2bpy); X = MeCN or pyridine (py)] are efficient mediators of glucose oxidase (GO) from Aspergillus niger and horseradish peroxidase (HRP). Their redox potentials in an aqueous buffer are in the range 0.15-0.35 V versus SCE, and the rate constants for the oxidation GO(red) (where red indicates reduced) by the electrochemically generated RuIII species equal (1.7-2.5) x 10(6) M(-1) s(-1) at pH 7 and 25 degrees C. The redox potentials of all complexes decrease cathodically by 0.4-0.6 V upon irradiation by visible light because of the photoinduced solvolysis of acetonitrile or py ligands. These in situ generated species display an even better mediating performance with HRP, although their behavior toward GO is different. The loading of a ruthenium unit into the protein interior brings about large catalytic currents in a self-assembled system GO-Ru-D-glucose. The estimated rate constant for intramolecular electron transfer from FADH2 of the active site at RuIII, k(intra), equals 4.4 x 10(3) s(-1). This suggests that the distance between the redox partners is around 19 A. The value of 21 A was obtained through the docking analysis of a possible closest-to-FAD localization of a Ru-containing fragment derived from the irradiated complex cis-[Ru(o-C6H4-py)-(phen)(MeCN)2]PF6. The operational stability of the GO-Ru assemblies depends on the nature of complex used, the highest being observed for cis-[Ru(o-C6H4-py)(Me2-bpy)(MeCN)2]PF6 (2). UV-vis studies of interaction of 2 with GO revealed photomechanical oscillations in the system GO-Ru-D-glucose. When irradiated complex 2 is mixed with GO and D-glucose, the absorbance at 510 nm increases because of the enzymatic reduction of RuIII to RuII. The absorbance drops rapidly and then increases as in the first cycle after shaking the reaction solution. Many cycles are possible, and the rate of absorbance increase does not depend on a cycle number. A plausible mechanism of the oscillations is presented.},
	biburl = {http://www.bibsonomy.org/bibtex/2b8b5d7e8d44fe8113b3edb93dc23299e/biblio24},
	keywords = {gox hrp ruthenium}
}

@article{citeulike:688075,
        title = {Cyclometalated ruthenium(II) complexes as efficient redox mediators in peroxidase catalysis.},
        address = {Department of Chemical Enzymology, Faculty of Chemistry, MV Lomonosov Moscow State University, 119899, Moscow, Russia.},
        author = {I. S. Alpeeva and V. S. Soukharev and L. Alexandrova and N. V. Shilova and N. V. Bovin and E. Csöregi and A. D. Ryabov and I. Y. Sakharov},
        journal = {J Biol Inorg Chem},
        month = {July},
        number = 6,
        pages = {683--688},
        volume = 8,
        year = 2003,
        url = {http://dx.doi.org/10.1007/s00775-003-0467-2},
        id = {688075},
	issn = {0949-8257},
	priority = {2},
	doi = {10.1007/s00775-003-0467-2},
	abstract = {Cyclometalated ruthenium(II) complexes, [Ru(II)(C~N)(N~N)(2)]PF(6) [HC~N=2-phenylpyridine (Hphpy) or 2-(4'-tolyl)pyridine; N~N=2,2'-bipyridine, 1,10-phenanthroline, or 4,4'-dimethyl-2,2'-bipyridine], are rapidly oxidized by H(2)O(2) catalyzed by plant peroxidases to the corresponding Ru(III) species. The commercial isoenzyme C of horseradish peroxidase (HRP-C) and two recently purified peroxidases from sweet potato (SPP) and royal palm tree (RPTP) have been used. The most favorable conditions for the oxidation have been evaluated by varying the pH, buffer, and H(2)O(2) concentrations and the apparent second-order rate constants ( k(app)) have been measured. All the complexes studied are oxidized by HRP-C at similar rates and the rate constants k(app) are identical to those known for the best substrates of HRP-C (10(6)-10(7) M(-1) s(-1)). Both cationic (HRP-C) and anionic (SPP and RPTP) peroxidases show similar catalytic efficiency in the oxidation of the Ru(II) complexes. The mediating capacity of the complexes has been evaluated using the SPP-catalyzed co-oxidation of [Ru(II)(phpy)(bpy)(2)]PF(6) and catechol as a poor peroxidase substrate as an example. The rate of enzyme-catalyzed oxidation of catechol increases more than 10000-fold in the presence of the ruthenium complex. A simple routine for calculating the rate constant k(c) for the oxidation of catechol by the Ru(III) complex generated enzymatically from [Ru(II)(phpy)(bpy)(2)](+) is proposed. It is based on the accepted mechanism of peroxidase catalysis and involves spectrophotometric measurements of the limiting Ru(II) concentration at different concentrations of catechol. The calculated k(c) value of 0.75 M(-1) s(-1) shows that the cyclometalated Ru(II) complexes are efficient mediators in peroxidase catalysis.},
	biburl = {http://www.bibsonomy.org/bibtex/2544b70ab4eb21c8eb6f7dbbdb4cabb2c/biblio24},
	keywords = {hrp ruthenium}
}

@article{citeulike:693526,
        title = {An amperometric immunosensor based on an electrochemically pretreated carbon-paraffin electrode for complement III (C3) assay.},
        address = {State Key Laboratory for Chemo/Biosensing Technology and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, PR China.},
        author = {Y. M. Zhou and S. Q. Hu and G. L. Shen and R. Q. Yu},
        journal = {Biosens Bioelectron},
        month = {April},
        number = 4,
        pages = {473--481},
        volume = 18,
        year = 2003,
        url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=12604265},
        id = {693526},
	issn = {0956-5663},
	priority = {2},
	abstract = {An electrochemical immunosensor based on the adsorption of anti-complement III antibody onto an electrochemical pretreated carbon-paraffin electrode has been proposed for the detection of complement III (C(3)). The competitive immunoassay format was adopted with horseradish peroxide-C(3) (HRP-C(3)) as a tracer, 3,3'5,5'-tetramethylbenzidine (TMB) and hydrogen peroxide as the enzyme substrates. In order to measure the amount of HRP-C(3) binding onto the electrode surface, the product of the enzyme catalytic reaction was detected at 100 mV (vs. Ag/AgCl reference electrode). The system was optimized to realize a reliable determination of C(3) in the range of 0.06-10 microg/ml. It exhibits some advantages, such as simplicity of fabrication, rapidity of measurement, and satisfactory sensitivity and reproducibility.},
	biburl = {http://www.bibsonomy.org/bibtex/216722cbd8fbe45ea348115e068481538/biblio24},
	keywords = {immunoassay immunoelectrode hrp electrochemistry competition amperometry}
}