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https://doi.org/10.5562/cca2488

Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes

Barbara Chiavarino ; Dipartimento di Chimica e Tecnologie del Farmaco, Università di Roma “La Sapienza”, P. le A. Moro 5, I-00185, Roma, Italy
Maria Elisa Crestoni ; Dipartimento di Chimica e Tecnologie del Farmaco, Università di Roma “La Sapienza”, P. le A. Moro 5, I-00185, Roma, Italy
Simonetta Fornarini ; Dipartimento di Chimica e Tecnologie del Farmaco, Università di Roma “La Sapienza”, P. le A. Moro 5, I-00185, Roma, Italy

Puni tekst: engleski, pdf (955 KB) str. 307-314 preuzimanja: 535* citiraj
APA 6th Edition
Chiavarino, B., Crestoni, M.E. i Fornarini, S. (2014). Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes. Croatica Chemica Acta, 87 (4), 307-314. https://doi.org/10.5562/cca2488
MLA 8th Edition
Chiavarino, Barbara, et al. "Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes." Croatica Chemica Acta, vol. 87, br. 4, 2014, str. 307-314. https://doi.org/10.5562/cca2488. Citirano 20.09.2019.
Chicago 17th Edition
Chiavarino, Barbara, Maria Elisa Crestoni i Simonetta Fornarini. "Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes." Croatica Chemica Acta 87, br. 4 (2014): 307-314. https://doi.org/10.5562/cca2488
Harvard
Chiavarino, B., Crestoni, M.E., i Fornarini, S. (2014). 'Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes', Croatica Chemica Acta, 87(4), str. 307-314. https://doi.org/10.5562/cca2488
Vancouver
Chiavarino B, Crestoni ME, Fornarini S. Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes. Croatica Chemica Acta [Internet]. 2014 [pristupljeno 20.09.2019.];87(4):307-314. https://doi.org/10.5562/cca2488
IEEE
B. Chiavarino, M.E. Crestoni i S. Fornarini, "Intrinsic Properties of Nitric Oxide Binding to Ferrous and Ferric Hemes", Croatica Chemica Acta, vol.87, br. 4, str. 307-314, 2014. [Online]. https://doi.org/10.5562/cca2488

Sažetak
Gas phase studies offer an ideal medium whereby structural and reactivity properties of charged spe-cies may be unveiled in the absence of solvent, matrix or counterion effects. In this environment NO binds to iron(II)- and iron(III)-hemes with comparable kinetics and equilibrium parameters, conclu-sively elucidating the factors determining the widely different affinity in protic solvents or in heme proteins. IRMPD spectroscopy of the isolated species provides unambiguous characterization of the gaseous
nitrosyl heme complexes.

Ključne riječi
five-coordinate hemes; nitrosyl complexes; FT-ICR mass spectrometry; IR spectroscopy; NO addition kinetics; metallobiomolecules

Hrčak ID: 131522

URI
https://hrcak.srce.hr/131522

Posjeta: 741 *