Registro:

Referencias:

• Rogers, K.R., Recent Advances in Biosensor Techniques for Environmental Monitoring (2006) Anal. Chim. Acta, 568, pp. 222-231
• Stock, A.M., Robinson, V.L., Goudreau, P.N., Two-Component Signal Transduction (2000) Annu. Rev. Biochem., 69, pp. 183-215
• Chan, M.K., Recent Advances in Heme-Protein Sensors (2001) Curr. Opin. Chem. Biol., 5, pp. 216-222
• Szurmant, H., Ordal, G.W., Diversity in Chemotaxis Mechanisms among the Bacteria and Archaea (2004) Microbiol. Mol. Biol. Rev., 68, pp. 301-319
• Wadhams, G.H., Armitage, J.P., Making Sense of It All: Bacterial Chemotaxis (2004) Nat. Rev. Mol. Cell. Biol., 5, pp. 1024-1037
• Fu, R., Wall, J.D., Voordouw, G., DcrA, a c-Type Heme-Containing Methyl-Accepting Protein from Desulfovibrio vulgaris Hildenborough, Senses the Oxygen Concentration or Redox Potential of the Environment (1994) J. Bacteriol., 176, pp. 344-350
• Hao, B., Isaza, C., Arndt, J., Soltis, M., Chan, M.K., Structure-Based Mechanism of O2 Sensing and Ligand Discrimination by the FixL Heme Domain of Bradyrhizobium japonicum (2002) Biochemistry, 41, pp. 12952-12958
• Yoshioka, S., Kobayashi, K., Yoshimura, H., Uchida, T., Kitagawa, T., Aono, S., Biophysical Properties of a c-Type Heme in Chemotaxis Signal Transducer Protein DcrA (2005) Biochemistry, 44, pp. 15406-15413
• Londer, Y.Y., Dementieva, I.S., Dausilio, C.A., Pokkuluri, P.R., Schiffer, M., Characterization of a c-Type Heme-containing PAS Sensor Domain from Geobacter sulfurreducens Representing a Novel Family of Periplasmic Sensors in Geobacteraceae and Other Bacteria (2006) FEMS Microbiol. Lett., 258, pp. 173-181
• Pokkuluri, P.R., Pessanha, M., Londer, Y.Y., Wood, S.J., Duke, N.E.C., Wilton, R., Catarino, T., Schiffer, M., Structures and Solution Properties of Two Novel Periplasmic Sensor Domains with c-Type Heme from Chemotaxis Proteins of Geobacter sulfurreducens: Implications for Signal Transduction (2008) J. Mol. Biol., 377, pp. 1498-1517
• Antonini, E., Brunori, M., (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, , North-Holland Publishing Co: Amsterdam
• Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., Simmerling, C., Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters (2006) Proteins. Struct., Funct. Genet., 65, pp. 712-725
• Bikiel, D.E., Boechi, L., Capece, L., Crespo, A., De Biase, P.M., Di Lella, S., Gonzalez Lebrero, M.C., Estrin, D.A., Modeling Heme Proteins Using Atomistic Simulations (2006) Phys. Chem. Chem. Phys., 8, pp. 5611-5628
• Capece, L., Estrin, D.A., Marti, M.A., Dynamical Characterization of the Heme NO Oxygen Binding (HNOX) Domain. Insight into Soluble Guanylate Cyclase Allosteric Transition (2008) Biochemistry, 47, pp. 9416-9427
• De Biase, P.M., Paggi, D.A., Doctorovich, F., Hildebrandt, P., Estrin, D.A., Murgida, D.H., Marti, M.A., Molecular Basis for the Electric Field Modulation of Cytochrome c Structure and Function (2009) J. Am. Chem. Soc., 131, pp. 16248-16256
• Marti, M.A., Crespo, A., Capece, L., Boechi, L., Bikiel, D.E., Scherlis, D.A., Estrin, D.A., Dioxygen Affinity in Heme Proteins Investigated Bycomputer Simulation (2006) J. Inorg. Biochem., 100, pp. 761-770
• Crespo, A., Scherlis, D.A., Marti, M.A., Ordejón, P., Roitberg, A.E., Estrin, D.A., A DFT-Based QM-MM Approach Designed for the Treatment of Large Molecular Systems: Application to Chorismate Mutase (2003) J. Phys. Chem. B, 107, pp. 13728-13736
• Siebert, F., Hildebrandt, P., (2008) Vibrational Spectroscopy in Life Science, , Wiley-VCH Verlag GmbH and Co., KGaA: Weinheim
• Ioanoviciu, A., Yukl, E.T., Moenne-Loccoz, P., De Montellano, P.R., Devs, a Heme-Containing Two-Component Oxygen Sensor of Mycobacterium tuberculosis (2007) Biochemistry, 46, pp. 4250-4260
• Inagaki, S., Masuda, C., Akaishi, T., Nakajima, H., Yoshioka, S., Ohta, T., Pal, B., Aono, S., Spectroscopic and Redox Properties of a CooA Homologue from Carboxydothermus hydrogenoformans (2005) J. Biol. Chem., 280, pp. 3269-3274
• Karow, D.S., Pan, D., Davis, J.H., Behrends, S., Mathies, R.A., Marletta, M.A., Characterization of Functional Heme Domains from Soluble Guanylate Cyclase (2005) Biochemistry, 44, pp. 16266-16274
• Reynolds, M.F., Parks, R.B., Burstyn, J.N., Shelver, D., Thorsteinsson, M.V., Kerby, R.L., Roberts, G.P., Spiro, T.G., Electronic Absorption, EPR, and Resonance Raman Spectroscopy of CooA, a CO-Sensing Transcription Activator from R. rubrum, Reveals a Five-Coordinate NO-Heme (2000) Biochemistry, 39, pp. 388-396
• Vogel, K.M., Hu, S., Spiro, T.G., Dierks, E.A., Yu, A.E., Burstyn, J.N., Variable Forms of Soluble Guanylyl Cyclase: Protein-Ligand Interactions and the Issue of Activation by Carbon Monoxide (1999) J. Biol. Inorg. Chem., 4, pp. 804-813
• Andrew, C.R., Green, E.L., Lawson, D.M., Eady, R.R., Resonance Raman Studies of Cytochrome c Support the Binding of NO and CO to Opposite Sides of the Heme: Implications for Ligand Discrimination in Heme-Based Sensors (2001) Biochemistry, 40, pp. 4115-4122
• Boon, E.M., Davis, J.H., Tran, R., Karow, D.S., Huang, S.H., Pan, D., Miazgowicz, M.M., Marletta, M.A., Nitric Oxide Binding to Prokaryotic Homologs of the Soluble Guanylate Cyclase ?1 H-NOX Domain (2006) J. Biol. Chem., 281, pp. 21892-21902
• Andrew, C.R., Kemper, L.J., Busche, T.L., Tiwari, A.M., Kecskes, M.C., Stafford, J.M., Croft, L.C., Eady, R.R., Accessibility of the Distal Heme Face, Rather Than Fe-His Bond Strength, Determines the Heme-Nitrosyl Coordination Number of Cytochromes c : Evidence from Spectroscopic Studies (2005) Biochemistry, 44, pp. 8664-8672
• Lukat-Rodgers, G.S., Rodgers, K.R., Characterization of Ferrous FixL-Nitric Oxide Adducts by Resonance Raman Spectroscopy (1997) Biochemistry, 36, pp. 4178-4187
• Ford, P.C., Fernandez, B.O., Lim, M.D., Mechanism of Reductive Nitrosylation in Iron and Copper Models Relevant to Biological Systems (2005) Chem. Rev., 105, pp. 2439-2455
• Ray, G.B., Li, X.Y., Ibers, J.A., Sessler, J.L., Spiro, T.G., How Far Can Proteins Bend the FeCO Unit? Distal Polar and Steric Effects in Heme Proteins and Models (1994) J. Am. Chem. Soc., 116, pp. 162-176
• Martí, M.A., Scherlis, D.A., Doctorovich, F.A., Ordejón, P.A., Estrin, D.A., Modulation of NO Trans Effect in Heme Proteins: Implications in Guanylate Cyclase Activation (2003) J. Biol. Inorg. Chem., 8, pp. 595-600
• Marti, M.A., Capece, L., Crespo, A., Doctorovich, F., Estrin, D.A., Nitric Oxide Interaction with Cytochrome c and Its Relevance to Guanylate Cyclase. Why Does the Iron Histidine Bond Break (2005) J. Am. Chem. Soc., 127, pp. 7721-7728
• Marti, M.A., González Lebrero, M.C., Roitberg, A.E., Estrin, D.A., Bond or Cage Effect: How Nitrophorins Transport and Release Nitric Oxide (2008) J. Am. Chem. Soc., 130, pp. 1611-1618
• Swails, J.M., Meng, Y., Walker, F.A., Marti, M.A., Estrin, D.A., Roitberg, A.E., PH-Dependent Mechanism of Nitric Oxide Release in Nitrophorins 2 and 4 (2009) J. Phys. Chem. B, 113, pp. 1192-1201
• Cooper, C.E., Nitric oxide and iron proteins (1999) Biochim. Biophys. Acta, 1411, pp. 290-309
• Viola, F., Aime, S., Coletta, M., Desideri, A., Fasano, M., Paletti, S., Tarricone, C., Ascenzi, P., Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: A comparative study (1996) J. Inorg. Biochem., 62, pp. 213-222
• Jones, M.G., Bickar, D., Wilson, M.T., Brunori, M., Colosimo, A., Sarti, P., A re-examination of the reactions of cyanide with cytochrome c oxidase (1984) Biochem. J., 220, pp. 57-66
• Stone, J.R., Marletta, M.A., The ferrous heme of soluble guanylate cyclase: Formation of hexacoordinate complexes with carbon monoxide and nitrosomethane (1995) Biochemistry, 34, pp. 16397-16403
• Mayburd, A.L., Kassner, R.J., Mechanism and biological role of nitric oxide binding to cytochrome c (2002) Biochemistry, 41, pp. 11582-11591
• Kassner, R.J., Ligand binding properties of cytochromes c (1991) Biochim. Biophys. Acta, 1058, pp. 8-12

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------