Nitric oxide binding to ferric cytochrome P450: A computational study

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The interaction between nitric oxide (NO) and the active site of ferric cytochrome P450 was studied by means of density functional theory (DFT), at the generalized gradient approximation level, and of the SAM1 semiempirical method. The electrostatic effects of the protein environment were included i...

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Autor principal: Scherlis, D.A
Otros Autores: Cymeryng, C.B, Estrin, D.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2000
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-0034729030 
024 7 |2 cas  |a Cytochrome P-450 Enzyme System, 9035-51-2; Ferric Compounds; Nitric Oxide, 10102-43-9; Proteins; Water, 7732-18-5 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a INOCA 
100 1 |a Scherlis, D.A. 
245 1 0 |a Nitric oxide binding to ferric cytochrome P450: A computational study 
260 |c 2000 
270 1 0 |m Estrin, D.A.; Facultad Ciencias Exactas Naturales, Universidad de Buenos Aires, Ciudad Universitaria - Pab II, 1428 Buenos Aires, Argentina; email: dario@ql.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a note; Lewis, D.F., Pratt, J.M., (1998) Drug Metab. Rev., 30, p. 739 
504 |a Poulos, T.L., (1995) Curr. Opin. Struct. Biol., 5, p. 767 
504 |a Ortiz De Montellano, P.R., (1995) Cytochrome P-450: Structure, Mechanism and Biochemistry, , Plenum Press: New York 
504 |a Guengerich, F.P., MacDonald, T.L., (1990) FASEB J., 4, p. 2453 
504 |a Dawson, J.H., Sono, M., (1987) Chem. Rev., 87, p. 1255 
504 |a Hanke, C.J., Drewett, J.G., Myers, C.R., Campbell, W.B., (1998) Endocrinology, 139, p. 4053 
504 |a Del Punta, K., Charreau, E.H., Pignataro, O., (1996) Endocrinology, 137, p. 5337 
504 |a Van Voorhis, B.J., Dunn, M.S., Snyder, G.D., Weiner, C.P., (1994) Endocrinology, 135, p. 1799 
504 |a Minamiyama, Y., Takemura, S., Imaoka, S., Funae, Y., Tanimoto, Y., Inoue, M., (1997) J. Pharmacol. Exp. Ther., 283, p. 1479 
504 |a Marques, H.M., Munro, O.Q., Grimmer, N.E., Levendis, D.C., Marsicano, F., Pattrick, G., Markoulides, T., (1995) J. Chem. Soc., Faraday Trans., 91, p. 1741 
504 |a Ghosh, A., Almlof, J., Lawrence Jr., Q., (1994) J. Phys. Chem., 98, p. 5576 
504 |a Ghosh, A., Bocian, D.F., (1996) J. Phys. Chem., 100, p. 6363 
504 |a Matsuzawa, N., Ata, M., Dixon, D.A., (1995) J. Phys. Chem., 99, p. 7698 
504 |a Jones, D.H., Hinman, A.S., Ziegler, T., (1993) Inorg. Chem., 32, p. 2092 
504 |a Havlin, R.H., Godbout, N., Salzmann, R., Wojdelski, M., Arnold, W., Schulz, C.E., Oldfield, E., (1998) J. Am. Chem. Soc., 120, p. 3144 
504 |a Spiro, G.T., Kozlowski, P.M., (1998) J. Am. Chem. Soc., 120, p. 4524 
504 |a Green, M.T., (1998) J. Am. Chem. Soc., 120, p. 10772 
504 |a Green, M.T., (1999) J. Am. Chem. Soc., 121, p. 7939 
504 |a Harris, D., Loew, G.H., Komornicki, A., (1997) J. Phys. Chem. A, 101, p. 3959 
504 |a Harris, D., Loew, G.H., Waskell, L., (1998) J. Am. Chem. Soc., 120, p. 4308 
504 |a Henson, N.J., Hay, P.J., Redondo, A., (1999) Inorg. Chem., 38, p. 1618 
504 |a Rovira, C., Kunc, K., Hutter, J., Ballone, P., Parrinello, M., (1997) J. Phys. Chem. A, 101, p. 8914 
504 |a Rovira, C., Parrinello, M., (1998) Int. J. Quantum Chem., 70, p. 387 
504 |a Rovira, C., Ballone, P., Parrinello, M., (1997) Chem. Phys. Lett., 271, p. 246 
504 |a De Groot, M.J., Havenith, R.W.A., Vinkers, H.M., Zwaans, R., Vermeulen, N.P.E., Van Lenthe, J.H., (1998) J. Comput.-Aided Mol. Des., 12, p. 183 
504 |a Yeom, H., Sligar, S.G., Li, H., Poulos, T.L., Fulco, A.J., (1995) Biochemistry, 34, p. 14733 
504 |a (1997) HyperChem, Release 5.1, , Pro; Hypercube, Inc.: Gainesville, FL 
504 |a Branden, C., Tooze, J., (1991) Introduction to Protein Structure, , Garland Publishing, Inc.: New York and London 
504 |a (1994) AMPAC 5.0, , 1994 Semichem: Shawnee, KS 
504 |a Holder, A.J., Ward, R., (1998) Abstr. Pap-Am. Chem. Soc., 216, p. 174 
504 |a White, D.A., Holder, A.J., Jie, C., (1998) Abstr. Pap-Am. Chem. Soc., 216, p. 182 
504 |a Estrin, D., Hamra, O.Y., Paglieri, L., Slep, L., Olabe, J., (1996) Inorg. Chem., 35, p. 6832 
504 |a Estrin, D., Baraldo, L., Slep, L., Barja, B., Olabe, J., Paglieri, L., Corongiu, G., (1996) Inorg. Chem., 35, p. 3897 
504 |a Taylor, J.C., Mueller, M.H., Hitterman, R.L., (1974) Acta Crystallogr., A26, p. 559 
504 |a Bottomley, F., White, P.S., (1979) Acta Crystallogr., B35, p. 2193 
504 |a Bray, M., Deeth, R., Paget, V., Sheen, P., (1996) Int. J. Quantum Chem., 61, p. 85 
504 |a Lang, G., Spartalian, K., Reed, C.A., Collman, L., (1978) J. Chem. Phys., 69, p. 5424 
504 |a Goff, H., La Mar, G.N., Reed, C.A., (1977) J. Am. Chem. Soc., 99, p. 3641 
504 |a Estrin, D.A., Corongiu, G., Clementi, E., (1993) METECC, Methods and Techniques in Computational Chemistry, , Clementi, E., Ed.; Stef: Cagliari, Italy 
504 |a Kohn, W., Sham, L.J., (1965) Phys. Rev., A140, p. 1133 
504 |a Becke, A.D., (1988) J. Chem. Phys., 88, p. 1053 
504 |a Godbout, N., Salahub, D.R., Andzelm, J., Wimmer, E., (1992) Can. J. Chem., 70, p. 560 
504 |a Andzelm, J., Radzio, E., Salahub, D.R., (1985) J. Comput. Chem., 6, p. 520 
504 |a Sim, F., Salahub, D.R., Chin, S., Dupuis, M., (1991) J. Chem. Phys., 95, p. 4317 
504 |a Sim, F., St-Amant, A., Papai, I., Salahub, D.R., (1992) J. Am. Chem. Soc., 114, p. 4391 
504 |a Vosko, S.H., Wilk, L., Nusair, M., (1980) Can. J. Phys., 58, p. 1200 
504 |a Perdew, P.W., (1986) Phys. Rev., B33, p. 8800 
504 |a (1986) Phys. Rev., B34, p. 7406. , erratum 
504 |a Becke, A.D., (1988) Phys. Rev., A38, p. 3098 
504 |a Elola, M.D., Laria, D., Estrin, D.A., (1999) J. Phys. Chem. A, 103, p. 5105 
504 |a Stanton, R.V., Little, L.R., Merz, K.M., (1995) J. Phys. Chem., 99, p. 17344 
504 |a Weiner, S.J., Kollman, P.A., Case, D.A., Singh, U.C., Ghio, C., Alagona, G., Profeta, S., Weiner, P., (1984) J. Am. Chem. Soc., 106, p. 765 
504 |a Weiner, S.J., Kollman, P.A., Nguyen, D.T., Case, D.A., (1986) J. Comput. Chem., 7, p. 230 
504 |a Parr, R.G., Yang, W., (1990) Density-Functional Theory of Atoms and Molecules, , Oxford University Press: New York 
504 |a Fukui, K., (1975) Theory of Orientation and Stereoselection, , SpringerVerlag: Berlin 
504 |a Fukui, K., (1987) Science, 218, p. 747 
504 |a Fukui, K., Yonezawa, T., Shingu, H., (1952) J. Chem. Phys., 20, p. 722 
504 |a Fukui, K., Yonezawa, T., Nagata, C., Shingu, H., (1954) J. Chem. Phys., 22, p. 1433 
504 |a Vasquez, G.B., Ji, X., Pechik, I., Fronticelli, C., Gilliland, G.L., X-ray Structure of Alpha-Oxy, Beta-(C1 12g)deoxy Human Hemoglobin, , http://www.ncbi.nlm.nih.gov, PDB Code: 1GBV. Protein Data Bank at the National Library of Medicine 
504 |a Collman, J.P., Sorrell, T.N., Hoffman, B.M., (1975) J. Am. Chem. Soc., 97, p. 913 
504 |a Collman, J.P., Sorrell, T.N., Hodgson, K.O., Kulshrestha, A.K., Strouse, C.E., (1977) J. Am. Chem. Soc., 99, p. 5180 
504 |a English, D.R., Hendrickson, D.N., Suslick, K.S., Eigenbrot, C.W., Scheldt, W.R., (1984) J. Am. Chem. Soc., 106, p. 7258 
504 |a Scheidt, W.R., Ellison, M.K., (1999) Acc. Chem. Res., 32, p. 350 
504 |a Enemark, J.H., Feltham, R.D., (1974) Coord. Chem. Rev., 13, p. 339 
504 |a Hoffmann, R., Chen, M.M.L., Elian, M., Rossi, A.R., Mingo, D.M.P., (1974) Inorg. Chem., 13, p. 2666 
504 |a Wayland, B.B., Olson, L.W., (1974) J. Am. Chem. Soc., 96, p. 6037 
504 |a Wong, M.W., Wiberg, K.B., Frisch, M.J., (1992) J. Am. Chem. Soc., 114, p. 1645 
504 |a Hoshino, M., Maeda, M., Konishi, R., Seki, H., Ford, P., (1996) J. Am. Chem. Soc., 118, p. 5702 
504 |a Ziegler, T., (1991) Chem. Rev., 91, p. 651 
504 |a Li, H., Poulos, T.L., (1995) Acta Crystallogr., D51, p. 21 
504 |a Schlichting, I., Jung, C., Schulze, H., (1997) FEBS Lett., 3, p. 253 
504 |a Sundaramoorthy, M., Terrer, J., Poulos, T.L., (1995) Structure (London), 3, p. 1367 
504 |a Peng, S.M., Ibers, J.A., (1976) J. Am. Chem. Soc., 98, p. 8032 
504 |a Scheidt, W.R., Prisse, M.E., (1975) J. Am. Chem. Soc., 97, p. 17 
504 |a Jameson, G.B., Rodley, G.A., Robinson, W.T., Gagne, R.R., Reed, C.A., Collman, J.P., (1978) Inorg. Chem., 17, p. 850 
504 |a Momenteau, M., Reed, C.A., (1994) Chem. Rev., 94, p. 659 
520 3 |a The interaction between nitric oxide (NO) and the active site of ferric cytochrome P450 was studied by means of density functional theory (DFT), at the generalized gradient approximation level, and of the SAM1 semiempirical method. The electrostatic effects of the protein environment were included in our DFT scheme by using a hybrid quantum classical approach. The active-site model consisted of an iron(III) porphyrin, the adjacent cysteine residue, and one coordinated water molecule. For this system, spin populations and relative energies for setected spin states were computed. Interestingly, the unpaired electron density, the HOMO, and the LUMO were found to be highly localized on the iron and in an appreciable extent on the sulfur coordinated to the metal. This provides central information about the reactivity of nitric oxide with the active site. Since the substitution of a molecule of H2O by NO has been proposed as being responsible for the inhibition of the cytochrome in the presence of nitric oxide, we have analyzed the thermodynamic feasibility of the ligand exchange process. The structure of the nitrosylated active site was partially optimized using SAM1. A low-spin ground state was obtained for the nitrosyl complex, with a linear Fe-N-O angle. The trends found in Fe-N-O angles and Fe-N lengths of the higher energy spin states provided a notable insight into the electronic configuration of the complex within the framework of the Enemark and Feltham formalism. In relation to the protein environment, it was assessed that the electrostatic field has significant effects on several computed properties. However, in both vacuum and protein environments, the ligand exchange reaction turned out to be exergonic and the relative orders of spin states of the relevant species were the same.  |l eng 
593 |a Depto. Quim. Inorg., Analitica Q., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina 
593 |a Depto. de Bioquímica Humana, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires, Argentina 
690 1 0 |a CYTOCHROME P450 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a FERRIC ION 
690 1 0 |a PROTEIN 
690 1 0 |a WATER 
690 1 0 |a ARTICLE 
690 1 0 |a CATALYSIS 
690 1 0 |a CHEMICAL BINDING 
690 1 0 |a ELECTRON TRANSPORT 
690 1 0 |a ENZYME ACTIVE SITE 
690 1 0 |a ENZYME BINDING 
690 1 0 |a GEOMETRY 
690 1 0 |a QUANTUM CHEMISTRY 
690 1 0 |a THERMODYNAMICS 
690 1 0 |a BINDING SITE 
690 1 0 |a CHEMICAL MODEL 
690 1 0 |a CHEMISTRY 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a CONFORMATION 
690 1 0 |a DRUG ANTAGONISM 
690 1 0 |a METABOLISM 
690 1 0 |a X RAY CRYSTALLOGRAPHY 
690 1 0 |a BINDING SITES 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a CRYSTALLOGRAPHY, X-RAY 
690 1 0 |a CYTOCHROME P-450 ENZYME SYSTEM 
690 1 0 |a FERRIC COMPOUNDS 
690 1 0 |a MODELS, CHEMICAL 
690 1 0 |a MOLECULAR CONFORMATION 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a PROTEINS 
690 1 0 |a THERMODYNAMICS 
690 1 0 |a WATER 
700 1 |a Cymeryng, C.B. 
700 1 |a Estrin, D.A. 
773 0 |d 2000  |g v. 39  |h pp. 2352-2359  |k n. 11  |p Inorg. Chem.  |x 00201669  |w (AR-BaUEN)CENRE-60  |t Inorganic Chemistry 
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856 4 0 |u https://doi.org/10.1021/ic991191d  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00201669_v39_n11_p2352_Scherlis  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v39_n11_p2352_Scherlis  |y Registro en la Biblioteca Digital 
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963 |a VARI 
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