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Measuring the cytochrome c nitrite reductase activity—practical considerations ...
Silveira, Célia M.; Besson, Stéphane; Moura, Isabel; Moura, José J. G.; Almeida, M. G.Hindawi Publishing Corporation Bioinorganic Chemistry and Applications Volume 2010, Article ID 634597, 8 pages ; The cytochrome c nitrite reductase (ccNiR) from Desulfovibrio desulfuricans ATCC 27774 is able to reduce nitrite to ammonia in a six-electron transfer reaction. Although extensively characterized from the spectroscopic and structural points-of-view, some of its kinetic aspects are still under explor...
Biochemical and spectroscopic characterization of the membrane-bound nitrate re...
Correia, Cristina; Besson, Stéphane; Brondino, Carlos D.; González, Pablo J.; Lampreia, Jorge; Moura, Isabel; Moura, José J. G.J Biol Inorg Chem (2008) 13:1321–1333 DOI 10.1007/s00775-008-0416-1 ; Membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617 can be solubilized in either of two ways that will ultimately determine the presence or absence of the small (Iota) subunit. The enzyme complex (NarGHI) is composed of three subunits with molecular masses of 130, 65, and 20 kDa. This enzyme contains approximately 14...
Copper-containing nitrite reductase from Pseudomonas chlororaphis DSM 50135
Moura, Isabel; Pinho, Dora; Besson, Stéphane; Brondino, Carlos D.; Castro, Baltazar deEur. J. Biochem. 271, 2361–2369 (2004) ; The nitrite reductase (Nir) isolated from Pseudomonas chlororaphis DSM 50135 is a blue enzyme, with type 1 and type 2 copper centers, as in all copper-containing Nirs described so far. For the first time, a direct determination of the reduction potentials of both copper centers in a Cu-Nir was performed: type 2 copper (T2Cu), 172 mV and type 1 copper (T1Cu), 298 mV at p...
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