Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa

Journal of Molecular Biology
K BrownM Tegoni

Abstract

The nitrite reductase (NIR) from Pseudomonas aeruginosa (NIR-Pa) is a soluble enzyme catalysing the reduction of nitrite (NO2(-)) to nitric oxide (NO). The enzyme is a 120 kDa homodimer, in which the monomers carry a c-heme domain and a d(1)-heme domain. The structures of the enzyme in both the oxidised and reduced state were solved previously and indicate His327 and His369 as putative catalytic residues. The kinetic characterisation of site-directed mutants has shown that the substitution of either one of these two His with Ala dramatically reduces the physiologically relevant reactivity towards nitrite, leaving the reactivity towards oxygen unaffected. The three-dimensional structures of P. aeruginosa NIR mutant H327A, and H369A in complex with NO have been solved by multiple wavelength anomalous dispersion (MAD), using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60 degrees rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d(1)-heme remains 21 A...Continue Reading

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Citations

Feb 7, 2002·Biochemical and Biophysical Research Communications·Wenliang SunFrancesca Cutruzzolà
Jun 13, 2003·Proceedings of the National Academy of Sciences of the United States of America·Ole FarverIsrael Pecht
Aug 15, 2014·Biochemical and Biophysical Research Communications·Serena RinaldoFrancesca Cutruzzolà
Jan 27, 2011·Biochemical Society Transactions·Serena RinaldoFrancesca Cutruzzolà
Apr 4, 2014·Chemical Reviews·Luisa B Maia, José J G Moura
May 11, 2005·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Scot WherlandIsrael Pecht
Jun 9, 2020·Acta Crystallographica. Section F, Structural Biology Communications·Thomas Klünemann, Wulf Blankenfeldt
Apr 26, 2016·Nitric Oxide : Biology and Chemistry·Lei-Bin WuXiangshi Tan
Jun 12, 2003·Chemical Reviews·James W Whittaker
Feb 12, 2011·Journal of the American Chemical Society·Marina RadoulDaniella Goldfarb

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