NDLI: Intramolecular Electron Transfer in Pseudomonas aeruginosa cd 1 Nitrite Reductase: Thermodynamics and Kinetics

Content Provider	PubMed Central
Author	Farver, Ole Brunori, Maurizio Francesca, Cutruzzolà Rinaldo, Serena Scot, Wherland Pecht, Israel
Copyright Year	2009
Abstract	The cd 1 nitrite reductases, which catalyze the reduction of nitrite to nitric oxide, are homodimers of 60 kDa subunits, each containing one heme-c and one heme-d 1. Heme-c is the electron entry site, whereas heme-d 1 constitutes the catalytic center. The 3D structure of Pseudomonas aeruginosa nitrite reductase has been determined in both fully oxidized and reduced states. Intramolecular electron transfer (ET), between c and d 1 hemes is an essential step in the catalytic cycle. In earlier studies of the Pseudomonas stutzeri enzyme, we observed that a marked negative cooperativity is controlling this internal ET step. In this study we have investigated the internal ET in the wild-type and His369Ala mutant of P. aeruginosa nitrite reductases and have observed similar cooperativity to that of the Pseudomonas stutzeri enzyme. Heme-c was initially reduced, in an essentially diffusion-controlled bimolecular process, followed by unimolecular electron equilibration between the c and d 1 hemes (k ET = 4.3 s−1 and K = 1.4 at 298K, pH 7.0). In the case of the mutant, the latter ET rate was faster by almost one order of magnitude. Moreover, the internal ET rate dropped (by ∼30-fold) as the level of reduction increased in both the WT and the His mutant. Equilibrium standard enthalpy and entropy changes and activation parameters of this ET process were determined. We concluded that negative cooperativity is a common feature among the cd 1 nitrite reductases, and we discuss this control based on the available 3D structure of the wild-type and the H369A mutant, in the reduced and oxidized states.
Related Links	http://dx.doi.org/10.1016/j.bpj.2008.12.3937
Starting Page	2849
File Format	PDF
ISSN	15420086
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	7
Volume Number	96
Language	English
Publisher	The Biophysical Society
Publisher Date	2009-04-08
Access Restriction	Open
Rights Holder	The Biophysical Society
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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