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Referencias:

• Bertini, I., Cavallaro, G., Rosato, A., Cytochrome c: occurrence and functions (2006) Chem. Rev., 106, pp. 90-115
• Sawyer, E.B., Barker, P.D., Continued surprises in the cytochrome c biogenesis story (2012) Protein Cell, 3, pp. 405-409
• Moore, G.R., Pettigrew, G.W., (1990) Cytochromes c. Evolutionary, Structural and Physicochemical Aspects, , Springer-Verlag, Berlin-Heidelberg-New York
• Kulikov, A.V., Shilov, E.S., Mufazalov, I.A., Gogvadze, V., Nedospasov, S.A., Zhivotovsky, B., Cytochrome c: the Achilles' heel in apoptosis (2012) Cell. Mol. Life Sci., 69, pp. 1787-1797
• Huttemann, M., Pecina, P., Rainbolt, M., Sanderson, T.H., Kagan, V.E., Samavati, L., Doan, J.W., Lee, I., The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis (2011) Mitochondrion, 11, pp. 369-381
• Ow, Y.L.P., Green, D.R., Hao, Z., Mak, T.W., Cytochrome c: functions beyond respiration (2008) Nat. Rev. Mol. Cell Biol., 9, pp. 532-542
• Liu, J., Chakraborty, S., Hosseinzadeh, P., Yu, Y., Tian, S., Petrik, I., Bhagi, A., Lu, Y., Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers (2014) Chem. Rev., 114, pp. 4366-4369
• Scott, R.A., Mauk, A.G., (1996) Cytochrome c: A Multidisciplinary Approach, , University Science Books, Sausalito, (Eds.)
• Soares, C.M., Baptista, A.M., Pereira, M.M., Teixeira, M., Investigation of protonatable residues in Rhodothermus marinus caa<inf>3</inf> haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa<inf>3</inf> haem-copper oxygen reductase (2004) J. Biol. Inorg. Chem., 9, pp. 124-134
• Sigurdson, H., Namslauer, A., Pereira, M.M., Teixeira, M., Brzezinski, P., Ligand binding and the catalytic reaction of cytochrome caa<inf>3</inf> from the thermophilic bacterium Rhodothermus marinus (2001) Biochemistry, 40, pp. 10578-10585
• Santana, M., Pereira, M.M., Elias, N.P., Soares, C.M., Teixeira, M., Gene cluster of Rhodothermus marinus high-potential iron-sulfur protein: oxygen oxidoreductase, a caa<inf>3</inf>-type oxidase belonging to the superfamily of heme-copper oxidases (2001) J. Bacteriol., 183, pp. 687-699
• Pereira, M.M., Verkhovskaya, M.L., Teixeira, M., Verkhovsky, M.I., The caa<inf>3</inf> terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump (2000) Biochemistry, 39, pp. 6336-6340
• Pereira, M.M., Santana, M., Soares, C.M., Mendes, J., Carita, J.N., Fernandes, A.S., Saraste, M., Teixeira, M., The caa<inf>3</inf> terminal oxidase of the thermohalophilic bacterium Rhodothermus marinus: a HiPIP : oxygen oxidoreductase lacking the key glutamate of the D-channel (1999) Biochim. Biophys. Acta Bioenerg., 1413, pp. 1-13
• Pereira, M.M., Sousa, F.L., Teixeira, M., Nyquist, R.M., Heberle, J., A tyrosine residue deprotonates during oxygen reduction by the caa<inf>3</inf> reductase from Rhodothermus marinus (2006) FEBS Lett., 580, pp. 1350-1354
• Srinivasan, V., Rajendran, C., Sousa, F.L., Melo, A.M.P., Saraiva, L.M., Pereira, M.M., Santana, M., Michel, H., Structure at 1.3 angstrom resolution of Rhodothermus marinus caa<inf>3</inf> cytochrome c domain (2005) J. Mol. Biol., 345, pp. 1047-1057
• Verissimo, A.F., Sousa, F.L., Baptista, A.M., Teixeira, M., Pereira, M.M., Thermodynamic redox behavior of the heme centers in A-type heme-copper oxygen reductases: comparison between the two subfamilies (2008) Biophys. J., 95, pp. 4448-4455
• Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., Teixeira, M., Murgida, D.H., Electron transfer dynamics of Rhodothermus marinus caa<inf>3</inf> cytochrome c domains on biomimetic films (2011) Phys. Chem. Chem. Phys., 13, pp. 18088-18098
• Stelter, M., Melo, A.M.P., Hreggvidsson, G.O., Hjorleifsdottir, S., Saraiva, L.M., Teixeira, M., Archer, M., Structure at 1.0 resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus (2010) J. Biol. Inorg. Chem., 15, pp. 303-313
• Grochol, J., Dronov, R., Lisdat, F., Hildebrandt, P., Murgida, D.H., Electron transfer in SAM/Cytochrome/polyelectrolyte hybrid systems on electrodes: a time-resolved surface-enhanced resonance Raman study (2007) Langmuir, 23, pp. 11289-11294
• Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S., Hildebrandt, P., Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy (2008) Phys. Chem. Chem. Phys., 10, pp. 5276-5286
• Kelly, S.M., Jess, T.J., Price, N.C., How to study proteins by circular dichroism (2005) Biochim. Biophys. Acta Protein Proteomics, 1751, pp. 119-139
• Stelter, M., Melo, A.M.P., Pereira, M.M., Gomes, C.M., Hreggvidsson, G.O., Hjorleifsdottir, S., Saraiva, L.M., Archer, M., A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23Å resolution of Rhodothermus marinus cytochrome c (2008) Biochemistry, 47, pp. 11953-11963
• Margoliash, E., Schejter, A., Cytochrome c (1966) Adv. Protein Chem., 21, pp. 113-286
• Schejter, A., Eaton, W.A., Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes (1984) Biochemistry, 23, pp. 1081-1084
• Latypov, R.F., Cheng, H., Roder, N.A., Zhang, J., Roder, H., Structural characterization of an equilibrium unfolding intermediate in cytochrome c (2006) J. Mol. Biol., 357, pp. 1009-1025
• Oellerich, S., Wackerbarth, H., Hildebrandt, P., Spectroscopic characterization of nonnative conformational states of cytochrome c (2002) J. Phys. Chem. B, 106, pp. 6566-6580
• Knapp, J.A., Pace, C.N., Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c (1974) Biochemistry, 13, pp. 1289-1294
• Yeh, S.R., Rousseau, D.L., Ligand exchange during unfolding of cytochrome c (1999) J. Biol. Chem., 274, pp. 17853-17859
• Street, T.O., Bolen, D.W., Rose, G.D., A molecular mechanism for osmolyte-induced protein stability (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 13997-14002
• Robinson, D.R., Jencks, W.P., The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds (1965) J. Am. Chem. Soc., 87, pp. 2462-2470
• Courtenay, E.S., Capp, M.W., Saecker, R.M., Record, M.T., Structural stability of binding sites: consequences for binding affinity and allosteric effects (2000) Proteins Struct. Funct. Genet., 41, pp. 63-71
• O'Brien, E.P., Dima, R.I., Brooks, B., Thirumalai, D., Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism (2007) J. Am. Chem. Soc., 129, pp. 7346-7353
• Mason, P.E., Brady, J.W., Neilson, G.W., Dempsey, C.E., The interaction of guanidinium ions with a model peptide (2007) Biophys. J., 93, pp. L04-L06
• Makhatadze, G.I., Privalov, P.L., Protein interactions with urea and guanidinium chloride; a calorimetric study (1992) J. Mol. Biol., 226, pp. 491-505
• Tiffany, M.L., Krimm, S., Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride (1973) Biopolymers, 12, pp. 575-587
• Lim, W.K., Rosgen, J., Englander, S.W., Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group (2009) Proc. Natl. Acad. Sci. U. S. A., 106, pp. 2595-2600
• Dempsey, C.E., Piggot, T.J., Mason, P.E., Dissecting contributions to the denaturant sensitivities of proteins (2005) Biochemistry, 44, pp. 775-781
• Smith, J.S., Scholtz, J.M., Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects (1996) Biochemistry, 35, pp. 7292-7297
• Alvarez-Paggi, D., Castro, M.A., Tortora, V., Castro, L., Radi, R., Murgida, D.H., Electrostatically driven second-sphere ligand switch between high and low reorganization energy forms of native cytochrome c (2013) J. Am. Chem. Soc., 135, pp. 4389-4397
• Murgida, D.H., Hildebrandt, P., Electron-transfer processes of cytochrome c at interfaces. New insights by surface-enhanced resonance Raman spectroscopy (2004) Acc. Chem. Res., 37, pp. 854-861
• Dopner, S., Hildebrandt, P., Resell, F.I., Mauk, A.G., Alkaline conformational transitions of ferricytochrome c studied by resonance Raman spectroscopy (1998) J. Am. Chem. Soc., 120, pp. 11246-11255
• Petrovic, J., Clark, R.A., Yue, H., Waldeck, D.H., Bowden, E.F., Impact of surface immobilization and solution ionic strength on the formal potential of immobilized cytochrome c (2005) Langmuir, 21, pp. 6308-6316
• Battistuzzi, G., Borsari, M., Sola, M., Francia, F., Redox thermodynamics of the native and alkaline forms of eukaryortic and bacterial class I cytochromes c (1997) Biochemistry, 36, pp. 16247-16258
• Khoa Ly, H., Sezer, M., Wisitruangsakul, N., Feng, J.J., Kranich, A., Millo, D., Weidinger, I.M., Hildebrandt, P., Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: electric field effects on structure, dynamics and function of cytochrome c (2011) FEBS J., 278, pp. 1382-1390
• Marcus, R.A., On theory of electron-transfer reactions. Unified treatment for homogeneous and electrode reactions (1965) J. Chem. Phys., 43, pp. 679-701
• Laviron, E., General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems (1979) J. Electroanal. Chem., 101, pp. 19-28
• Murgida, D.H., Hildebrandt, P., Redox and redox-coupled processes of heme proteins and enzymes at electrochemical interfaces (2005) Phys. Chem. Chem. Phys., 7, pp. 3773-3784
• Liu, B., Bard, A.J., Mirkin, M.V., Creager, S.E., Electron transfer at self-assembled monolayers measured by scanning electrochemical microscopy (2004) J. Am. Chem. Soc., 126, pp. 1485-1492
• Krishtalik, L.I., The medium reorganization energy for the charge transfer reactions in proteins (2011) Biochim. Biophys. Acta Bioenerg., 1807, pp. 1444-1456
• Mitra, D., Pelmenschikov, V., Guo, Y., Case, D.A., Wang, H., Dong, W., Tan, M.L., Cramer, S.P., Dynamics of the [4Fe-4S] cluster in Pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance raman spectroscopies, force field simulations, and density functional theory calculations (2011) Biochemistry, 50, pp. 5220-5235
• Sigfridsson, E., Olsson, M.H.M., Ryde, U., Inner-sphere reorganization energy of iron-sulfur clusters studied with theoretical methods (2001) Inorg. Chem., 40, pp. 2509-2519
• Kummerle, R., Gaillard, J., Kyritsis, P., Moulis, J.M., Intramolecular electron transfer in [4Fe-4S] proteins: estimates of the reorganization energy and electronic coupling in Chromatium vinosum ferredoxin (2001) J. Biol. Inorg. Chem., 6, pp. 446-451
• Jensen, K.P., Iron-sulfur clusters: why iron? (2006) J. Inorg. Biochem., 100, pp. 1436-1439
• Babini, E., Bertini, I., Borsari, M., Capozzi, F., Luchinat, C., Zhang, X., Moura, G.L.C., Gray, H.B., Bond-mediated electron tunneling in ruthenium-modified high-potential iron-sulfur protein (2000) J. Am. Chem. Soc., 122, pp. 4532-4533
• Capdevila, D.A., Marmisollé, W.A., Tomasina, F., Demichelli, V., Portela, M., Radi, R., Murgida, D.H., Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis (2015) Chem. Sci., 6, pp. 705-713
• Feng, J.J., Hildebrandt, P., Murgida, D.H., Silver nanocoral structures on electrodes: a suitable platform for protein-based bioelectronic devices (2008) Langmuir, 24, pp. 1584-1586
• Wang, B., Zhang, J.J., Pan, Z.Y., Tao, X.Q., Wang, H.S., A novel hydrogen peroxide sensor based on the direct electron transfer of horseradish peroxidase immobilized on silica-hydroxyapatite hybrid film (2009) Biosens. Bioelectron., 24, pp. 1141-1145
• Casalini, S., Battistuzzi, G., Borsari, M., Bortolotti, C.A., Di Rocco, G., Ranieri, A., Sola, M., Electron transfer properties and hydrogen peroxide electrocatalysis of cytochrome c variants at positions 67 and 80 (2010) J. Phys. Chem. B, 114, pp. 1698-1706
• Águila, S., Vidal-Limón, A.M., Alderete, J.B., Sosa-Torres, M., Vázquez-Duhalt, R., Unusual activation during peroxidase reaction of a cytochrome c variant (2013) J. Mol. Catal. B Enzymatic, pp. 187-192
• Battistuzzi, G., Bellei, M., Bortolotti, C.A., Sola, M., Redox properties of heme peroxidases (2010) Arch. Biochem. Biophys., 500, pp. 21-36
• Ranieri, A., Bernini, F., Bortolotti, C.A., Castellini, E., The Met80Ala point mutation enhances the peroxidase activity of immobilized cytochrome c (2012) Catal. Sci. Technol., 2, pp. 2206-2210
• Valderrama, B., Ayala, M., Vazquez-Duhalt, R., Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes (2002) Chem. Biol., 9, pp. 555-565
• Wang, L., Waldeck, D.H., Denaturation of cytochrome c and its peroxidase activity when immobilized on SAM films (2008) J. Phys. Chem. C, 112, pp. 1351-1356

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