Título:
Kinetics of nitrite reduction and peroxynitrite formation by ferrous heme in human cystathionine β-synthase
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Autor:
Carballal, S.
Cuevasanta, Ernesto
Yadav, P. K.
Gherasim, C.
Ballou, D. P.
Álvarez, Beatriz
Banerjee, Ruma
Cuevasanta, Ernesto
Yadav, P. K.
Gherasim, C.
Ballou, D. P.
Álvarez, Beatriz
Banerjee, Ruma
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Tipo de documento:
Artículo
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Palabras clave:
Heme
kinetics
Nitric oxide
Oxygen radicals
Superoxide ion
Hemeprotein
Nitrite
Oxygen
Peroxynitrite
kinetics
Nitric oxide
Oxygen radicals
Superoxide ion
Hemeprotein
Nitrite
Oxygen
Peroxynitrite
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Año de publicación:
2016
Contenido:
Resumen:
Cystathionine β-synthase (CBS) is a pyridoxal phosphate-dependent enzyme that catalyzes the condensation of homocysteine with serine or with cysteine to form cystathionine and either water or hydrogen sulfide, respectively. Human CBS possesses a noncatalytic heme cofactor with cysteine and histidine as ligands, which in its oxidized state is relatively unreactive. Ferric CBS (Fe(III)-CBS) can be reduced by strong chemical and biochemical reductants to Fe(II)-CBS, which can bind carbon monoxide (CO) or nitric oxide (NO·), leading to inactive enzyme. Alternatively, Fe(II)-CBS can be reoxidized by O2 to Fe(III)-CBS, forming superoxide radical anion (O2 -·). In this study, we describe the kinetics of nitrite (NO2·-) reduction by Fe(II)-CBS to form Fe(II)NO·-CBS. The second order rate constant for the reaction of Fe(II)-CBS with nitrite was obtained at low dithionite concentrations. Reoxidation of Fe(II)NO·-CBS by O2 showed complex kinetic behavior and led to peroxynitrite (ONOO-) formation, which was detected using the fluorescent probe, coumarin boronic acid. Thus, in addition to being a potential source of superoxide radical, CBS constitutes a previously unrecognized source of NO· and peroxynitrite.
Descripción:
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Editorial:
The American Society for Biochemistry and Molecular Biology
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Journal of Biological Chemistry, 2016, 291 (15), 8004-8013
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Citación:
Carballal, S., et al.Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase. Journal of Biological Chemistry, 2016, 291 (15), 8004-8013. doi: 10.1074/jbc.M116.718734
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0021-9258
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Licencia Creative Commons Atribución – No Comercial – Sin Derivadas (CC –BY-NC-ND 4.0)
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| Ficheros | Descripción | Tamaño | Formato | ||
|---|---|---|---|---|---|
| 101074jbcM116718734.pdf | — | 1.26 MB | Adobe PDF |