Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?

The Journal of Biological Chemistry
D NurizzoM Tegoni

Abstract

The structures of nitrite reductase from Paracoccus denitrificans GB17 (NiR-Pd) and Pseudomonas aeruginosa (NiR-Pa) have been described for the oxidized and reduced state (Fülöp, V., Moir, J. W. B., Ferguson, S. J., and Hajdu, J. (1995) Cell 81, 369-377; Nurizzo, D., Silvestrini, M. C., Mathieu, M., Cutruzzolà, F., Bourgeois, D., Fülöp, V., Hajdu, J., Brunori, M., Tegoni, M., and Cambillau, C. (1997) Structure 5, 1157-1171; Nurizzo, D., Cutruzzolà, F., Arese, M., Bourgeois, D., Brunori, M., Cambillau, C. , and Tegoni, M. (1998) Biochemistry 37, 13987-13996). Major conformational rearrangements are observed in the extreme states although they are more substantial in NiR-Pd. The four structures differ significantly in the c heme domains. Upon reduction, a His17/Met106 heme-ligand switch is observed in NiR-Pd together with concerted movements of the Tyr in the distal site of the d1 heme (Tyr10 in NiR-Pa, Tyr25 in NiR-Pd) and of a loop of the c heme domain (56-62 in NiR-Pa, 99-116 in NiR-Pd). Whether the reduction of the c heme, which undergoes the major rearrangements, is the trigger of these movements is the question addressed by our study. This conformational reorganization is not observed in the partially reduced species, in wh...Continue Reading

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Citations

Feb 7, 2002·Biochemical and Biophysical Research Communications·Wenliang SunFrancesca Cutruzzolà
Sep 21, 2001·Journal of Molecular Biology·K BrownM Tegoni
Jan 24, 2006·Biophysical Journal·Sophie Sacquin-Mora, Richard Lavery
Apr 4, 2014·Chemical Reviews·Luisa B Maia, José J G Moura
Jun 9, 2020·Acta Crystallographica. Section F, Structural Biology Communications·Thomas Klünemann, Wulf Blankenfeldt
Feb 12, 2011·Journal of the American Chemical Society·Marina RadoulDaniella Goldfarb
Feb 12, 2019·Chemical Reviews·Kazuo Kobayashi

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