Pure and Applied Chemistry

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• Ranieri Antonio, Bortolotti Carlo A., Battistuzzi Gianantonio, Borsari Marco, Paltrinieri Licia, Di Rocco Giulia, Sola Marco: Effect of motional restriction on the unfolding properties of a cytochrome c featuring a His/Met–His/His ligation switch. Metallomics 2014, 6, 874. <http://dx.doi.org/10.1039/c3mt00311f>
• Zhong F., Lisi G. P., Collins D. P., Dawson J. H., Pletneva E. V.: Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins. Proceedings of the National Academy of Sciences 2014, 111, E306. <http://dx.doi.org/10.1073/pnas.1317173111>
• Hagen Katharine D., Gillan James M., Im Sang-Choul, Landefeld Sally, Mead Griffin, Hiley Megan, Waskell Lucy A., Hill Michael G., Udit Andrew K.: Electrochemistry of mammalian cytochrome P450 2B4 indicates tunable thermodynamic parameters in surfactant films. Journal of Inorganic Biochemistry 2013, 129, 30. <http://dx.doi.org/10.1016/j.jinorgbio.2013.07.039>
• Warren Jeffrey J., Winkler Jay R., Gray Harry B.: Redox properties of tyrosine and related molecules. FEBS Letters 2012, 586, 596. <http://dx.doi.org/10.1016/j.febslet.2011.12.014>
• Ranieri Antonio, Battistuzzi Gianantonio, Borsari Marco, Bortolotti Carlo Augusto, Rocco Giulia Di, Sola Marco: pH and Solvent H/D Isotope Effects on the Thermodynamics and Kinetics of Electron Transfer for Electrode-Immobilized Native and Urea-Unfolded Stellacyanin. Langmuir 2012, 28, 15087. <http://dx.doi.org/10.1021/la303363h>
• Song Jie, Xu JiMing, Zhao PuSu, Lu LuDe, Bao JianChun: A hydrogen peroxide biosensor based on direct electron transfer from hemoglobin to an electrode modified with Nafion and activated nanocarbon. Microchim Acta 2011, 172, 117. <http://dx.doi.org/10.1007/s00604-010-0470-6>
• Liu Yang, Han Ting, Chen Chao, Bao Ning, Yu Chun-Mei, Gu Hai-Ying: A novel platform of hemoglobin on core–shell structurally Fe3O4@Au nanoparticles and its direct electrochemistry. Electrochimica Acta 2011, 56, 3238. <http://dx.doi.org/10.1016/j.electacta.2011.01.037>
• Levin Benjamin D., Can Mehmet, Bowman Sarah E. J., Bren Kara L., Elliott Sean J.: Methionine Ligand Lability in Bacterial Monoheme Cytochromes c: An Electrochemical Study. Chem B 2011, 115, 11718. <http://dx.doi.org/10.1021/jp203292h>
• Battistuzzi Gianantonio, Bellei Marzia, Vlasits Jutta, Banerjee Srijib, Furtmüller Paul G., Sola Marco, Obinger Christian: Redox thermodynamics of lactoperoxidase and eosinophil peroxidase. Archives of Biochemistry and Biophysics 2010, 494, 72. <http://dx.doi.org/10.1016/j.abb.2009.11.021>
• Chen Yu, Yang Xiao-Jing, Guo Li-Rong, Li Jing, Xia Xing-Hua, Zheng Li-Min: Direct electrochemistry and electrocatalysis of hemoglobin at three-dimensional gold film electrode modified with self-assembled monolayers of 3-mercaptopropylphosphonic acid. Analytica Chimica Acta 2009, 644, 83. <http://dx.doi.org/10.1016/j.aca.2009.04.027>
• Battistuzzi Gianantonio, Borsari Marco, Dennison Christopher, Li Chan, Ranieri Antonio, Sola Marco, Yanagisawa Sachiko: Active site loop dictates the thermodynamics of reduction and ligand protonation in cupredoxins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2009, 1794, 995. <http://dx.doi.org/10.1016/j.bbapap.2009.02.001>
• Ranieri Antonio, Battistuzzi Gianantonio, Borsari Marco, Casalini Stefano, Fontanesi Claudio, Monari Stefano, Siwek Michal Jan, Sola Marco: Thermodynamics and kinetics of the electron transfer process of spinach plastocyanin adsorbed on a modified gold electrode. Journal of Electroanalytical Chemistry 2009, 626, 123. <http://dx.doi.org/10.1016/j.jelechem.2008.12.001>
• Mader Elizabeth A., Manner Virginia W., Markle Todd F., Wu Adam, Franz James A., Mayer James M.: Trends in Ground-State Entropies for Transition Metal Based Hydrogen Atom Transfer Reactions. J Am Chem Soc 2009, 131, 4335. <http://dx.doi.org/10.1021/ja8081846>
• Lo Terence P., Murphy Michael E.P., Guy Guillemette J., Smith Michael, Brayer Gary D.: Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c. Protein Sci 2008, 4, 198. <http://dx.doi.org/10.1002/pro.5560040207>
• Monari Stefano, Battistuzzi Gianantonio, Borsari Marco, Millo Diego, Gooijer Cees, Zwan Gert, Ranieri Antonio, Sola Marco: Thermodynamic and kinetic aspects of the electron transfer reaction of bovine cytochrome c immobilized on 4-mercaptopyridine and 11-mercapto-1-undecanoic acid films. J Appl Electrochem 2008, 38, 885. <http://dx.doi.org/10.1007/s10800-008-9493-7>
• Sainz Germaine, Jakoncic Jean, Sieker Larry C., Stojanoff Vivian, Sanishvili Nukri, Asso Marcel, Bertrand Patrick, Armengaud Jean, Jouanneau Yves: Structure of a [2Fe–2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe–S cluster biogenesis and conformational changes observed upon reduction. J Biol Inorg Chem 2006, 11, 235. <http://dx.doi.org/10.1007/s00775-005-0069-2>
• Battistuzzi Gianantonio, Bellei Marzia, Rienzo Francesca, Sola Marco: Redox properties of the Fe3+/Fe2+ couple in Arthromyces ramosus class II peroxidase and its cyanide adduct. J Biol Inorg Chem 2006, 11, 586. <http://dx.doi.org/10.1007/s00775-006-0108-7>
• Battistuzzi G., Bellei M., Borsari M., Di Rocco G., Ranieri A., Sola M.: Axial ligation and polypeptide matrix effects on the reduction potential of heme proteins probed on their cyanide adducts. J Biol Inorg Chem 2005, 10, 643. <http://dx.doi.org/10.1007/s00775-005-0014-4>
• Battistuzzi Gianantonio, Bellei Marzia, Leonardi Alan, Pierattelli Roberta, Candia Ariel, Vila Alejandro J., Sola Marco: Reduction thermodynamics of the T1 Cu site in plant and fungal laccases. J Biol Inorg Chem 2005, 10, 867. <http://dx.doi.org/10.1007/s00775-005-0035-z>
• Borsari M., Bellei M., Tavagnacco C., Peressini S., Millo D., Costa G.: Redox thermodynamics of cytochrome c in mixed water–organic solvent solutions. Inorg Chim Ada 2003, 349, 182. <http://dx.doi.org/10.1016/S0020-1693(03)00043-4>
• Battistuzzi Gianantonio, Borsari Marco, Sola Marco: Medium and Temperature Effects on the Redox Chemistry of Cytochromec. Eur J Inorg Chem 2001, 2001, 2989. <http://dx.doi.org/10.1002/1099-0682(200112)2001:12<2989::AID-EJIC2989>3.0.CO;2-E>
• Farver O., Zhang J., Chi Q., Pecht I., Ulstrup J.: Deuterium isotope effect on the intramolecular electron transfer in Pseudomonas aeruginosa azurin. Proceedings of the National Academy of Sciences 2001, 98, 4426. <http://dx.doi.org/10.1073/pnas.071043798>
• Reipa Vytas, Holden Marcia J, Mayhew Martin P, Vilker Vincent L: Temperature dependence of the formal reduction potential of putidaredoxin. Biochim Biophys Acta Bioenerg 2000, 1459, 1. <http://dx.doi.org/10.1016/S0005-2728(00)00108-0>
• Lindgren Annika, Larsson Ted, Ruzgas Tautgirdas, Gorton Lo: Direct electron transfer between the heme of cellobiose dehydrogenase and thiol modified gold electrodes. Journal of Electroanalytical Chemistry 2000, 494, 105. <http://dx.doi.org/10.1016/S0022-0728(00)00326-0>
• Venturi Margherita, Credi Alberto, Balzani Vincenzo: Electrochemistry of coordination compounds: an extended view. Coord Chem Rev - 1999, 185-186, 233. <http://dx.doi.org/10.1016/S0010-8545(98)00271-9>
• Wittung-Stafshede Pernilla: Effect of redox state on unfolding energetics of heme proteins. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1999, 1432, 401. <http://dx.doi.org/10.1016/S0167-4838(99)00116-8>
• Brill Arthur S.: Elastic control of electron transfer enthalpy and intensity of light absorption by cupric blue proteins. biophys chem 1999, 80, 129. <http://dx.doi.org/10.1016/S0301-4622(99)00068-X>
• A. Feinberg Benjamin, Petro Lisa, Hock Gregory, Qin Wenying, Margoliash Emanuel: Using entropies of reaction to predict changes in protein stability: tyrosine-67-phenylalanine variants of rat cytochrome c and yeast Iso-1 cytochromes c. J  Pharm Biomed Anal 1999, 19, 115. <http://dx.doi.org/10.1016/S0731-7085(98)00291-X>
• Babini E., Borsari M., Capozzi F.: Thermodynamics of reduction of Chromatium vinosum high-potential iron-sulfur protein and its histidine depleted H42Q mutant. Inorg Chim Ada 1998, 275-276, 230. <http://dx.doi.org/10.1016/S0020-1693(98)00115-7>
• Heering H.A., Hagen W.R.: Complex electrochemistry of flavodoxin at carbon-based electrodes: results from a combination of direct electron transfer, flavin-mediated electron transfer and comproportionation. Journal of Electroanalytical Chemistry 1996, 404, 249. <http://dx.doi.org/10.1016/0022-0728(95)04248-2>
• Kyritsis Panayotis, Khozhuma Takamitsu, Sykes A.Geoffrey: Redox reactivity of the type 1 copper protein amicyanin from Thiobacillus versutus with its physiological partner cytochrome c550 and inter-protein cross-reaction studies. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1996, 1295, 245. <http://dx.doi.org/10.1016/0167-4838(96)00048-9>
• Barker Paul D., Butler Joanna L., de Oliveira Pedro, Hill H.Allen O., Hunt Nick I.: Direct electrochemical studies of cytochromes b562. Inorg Chim Ada 1996, 252, 71. <http://dx.doi.org/10.1016/S0020-1693(96)05299-1>
• Mines Gary A., Pascher Torbjörn, Lee Sonny C., Winkler Jay R., Gray Harry B.: Cytochrome c folding triggered by electron transfer. CHEM BIOL 1996, 3, 491. <http://dx.doi.org/10.1016/S1074-5521(96)90097-6>
• Steensma Elles, Heering Hendrik A., Hagen Wilfred R., Mierlo Carlo P. M.: Redox Properties of Wild-Type, Cys69Ala, and Cys69Ser Azotobacter Vinelandii Flavodoxin II as Measured by Cyclic Voltammetry and EPR Spectroscopy. Eur J Biochem 1996, 235, 167. <http://dx.doi.org/10.1111/j.1432-1033.1996.00167.x>
• Niu, Jianjun, Dong, Shaojun: Transmission Spectroelectrochemistry. REVAC 1996, 15, 1. <http://dx.doi.org/10.1515/REVAC.1996.15.1-2.1>
• Cai C.X., Ju H.X., Chen H.Y.: The effects of temperature and electrolyte on the redox potential of cytochrome c at a chemically modified microband gold electrode. Electrochimica Acta 1995, 40, 1109. <http://dx.doi.org/10.1016/0013-4686(95)00023-8>
• Mandal Subrata, Shukla Rameshwer, Bharadwaj Parimal K.: Modelling the blue protein active sites: Synthesis and characterization of CuN2S2 complexes showing rhombic EPR spectra and high CuII/CuI potential. J Polyhedron 1995, 14, 2063. <http://dx.doi.org/10.1016/0277-5387(95)00028-Q>
• Bertrand P., Asso M., Mbarki O., Camensuli P., More C., Guigliarelli B.: Individual redox characteristics and kinetic properties of the hemes in cytochromes c3: New methods of investigation. Biochemie 1994, 76, 524. <http://dx.doi.org/10.1016/0300-9084(94)90176-7>
• VERHAGEN Marc F. J. M., WOLBERT Ronnie B. G., HAGEN Wilfred R.: Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase. Eur J Biochem 1994, 221, 821. <http://dx.doi.org/10.1111/j.1432-1033.1994.tb18796.x>
• Murphy Michael E. P., Brayer Gary D., Fetrow Jacquelyn S., Burton Randall E.: The structure and function of omega loop A replacements in cytochrome c. Protein Sci 1993, 2, 1429. <http://dx.doi.org/10.1002/pro.5560020907>
• Qijin Chi, Shaojun Dong: Redox thermodynamics of cytochrome c at the bare glassy carbon electrode. Journal of Electroanalytical Chemistry 1993, 348, 377. <http://dx.doi.org/10.1016/0022-0728(93)80144-7>
• St. Clair Cynthia Strong, Ellis Walther R., Gray Harry B.: Spectroelectrochemistry of blue copper proteins: pH and temperature dependences of the reduction potentials of five azurins. Inorg Chim Ada 1992, 191, 149. <http://dx.doi.org/10.1016/S0020-1693(00)80341-2>
• LINK Thomas A., HAGEN Wilfred R., PIERIK Antonio J., ASSMANN Claus, JAGOW Gebhard: Determination of the redox properties of the Rieske [2Fe-2S] cluster of bovine heart bc1 complex by direct electrochemistry of a water-soluble fragment. Eur J Biochem 1992, 208, 685. <http://dx.doi.org/10.1111/j.1432-1033.1992.tb17235.x>
• Karlsson B.Göran, Aasa Roland, Malmström Bo G., Lundberg Lennart G.: Rack-induced bonding in blue copper proteins: Spectroscopic properties and reduction potential of the azurin mutant Met-121 → Leu. FEBS Letters 1989, 253, 99. <http://dx.doi.org/10.1016/0014-5793(89)80938-X>
• Pascher Torbjörn, Bergström Jörgen, Malmström Bo G., Vänngård Tore, Lundberg Lennart G.: Modification of the electron-transfer sites of Pseudomonas aeruginosa azurin by site-directed mutagenesis. FEBS Letters 1989, 258, 266. <http://dx.doi.org/10.1016/0014-5793(89)81670-9>
• Gui Yupeng, Kuwana Theodore, Valent O., Koryta J., Panoch M., Che Chi-Ming, Wong Kwok-Yin, Anson Fred C.: Electrochemistry and spectroelectrochemistry of cytochrome c at a platinum electrode. Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 1987, 226, 199. <http://dx.doi.org/10.1016/0022-0728(87)80044-X>
• Guss J.Mitchell, Harrowell Peter R., Murata Mitsuo, Norris Valerie A., Freeman Hans C.: Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values. Journal of Molecular Biology 1986, 192, 361. <http://dx.doi.org/10.1016/0022-2836(86)90371-2>
• King Garry C., Binstead Robert A., Wright Peter E.: NMR and kinetic characterization of the interaction between French bean plastocyanin and horse cytochrome c. Biochim Biophys Acta Bioenerg 1985, 806, 262. <http://dx.doi.org/10.1016/0005-2728(85)90104-5>
• Phani K.L.N., Narayan R., Heerman L., De Waele R., D'Olieslager W., Taniguchi Isao, Funatsu Toshihiro, Iseki Masahiro, Yamaguchi Hiroko, Yasukouchi Kazuo: Electrochemical reduction of O2 from molten acetamide at 85��C at mercury and at platinum electrodes. Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 1985, 193, 283. <http://dx.doi.org/10.1016/0022-0728(85)85072-5>
• Dreyer J. L.: Electron transfer in biological systems: an overview. CMLS Cell Mol Life Sci 1984, 40, 653. <http://dx.doi.org/10.1007/BF01949719>
• Toma Henrique E., Batista Alzir A.: Self-exchange rates and electron transfer kinetics of horse heart ferricytochrome C with amino acid-pentacyanoferrate(II) complexes. J  Inorg Biochem 1984, 20, 53. <http://dx.doi.org/10.1016/0162-0134(84)80005-7>
• Henry Yann, Bessières Philippe: Denitrification and nitrite reduction: Pseudomonas aeruginosa nitrite-reductase. Biochemie 1984, 66, 259. <http://dx.doi.org/10.1016/0300-9084(84)90005-1>
• Toma Henrique E., Murakami Roberto A.: Reduction of ferricytochrome-c by Co(II)-sepulchrate. Inorg Chim Ada 1984, 93, L33. <http://dx.doi.org/10.1016/S0020-1693(00)86792-4>
• Huang Yung-Yuan, Kimura Tokuji: Reduction potential and thermodynamic parameters of adrenodoxin by the use of an anaerobic thin-layer electrode. Analytical Biochemistry 1983, 133, 385. <http://dx.doi.org/10.1016/0003-2697(83)90099-4>
• Gray Harry B., Malmström Bo. G.: On the Relationship between Protein-Forced Ligand Fields and the Properties of Blue Copper Centers. Comments Inorg Chem 1983, 2, 203. <http://dx.doi.org/10.1080/02603598308078118>
• Matsuura Yoshiki, Takano Tsunehiro, Dickerson Richard E.: Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. Journal of Molecular Biology 1982, 156, 389. <http://dx.doi.org/10.1016/0022-2836(82)90335-7>
• Fultz Mary Lou, Durst Richard A.: Mediator compounds for the electrochemical study of biological redox systems: a compilation. Analytica Chimica Acta 1982, 140, 1. <http://dx.doi.org/10.1016/S0003-2670(01)95447-9>
• Wawrousek E.F., McArdle James V.: Spectroelectrochemistry of ferrioxamine B, ferrichrome, and ferrichrome A. J  Inorg Biochem 1982, 17, 169. <http://dx.doi.org/10.1016/S0162-0134(00)80097-5>