@article {10239, title = {Structural and mechanistic insights on nitrate reductases}, journal = {Protein Science}, volume = {24}, year = {2015}, note = {

ISI Document Delivery No.: DB1TNCoelho, Catarina Romao, Maria Joao
Life Sciences (LS)
Wiley-blackwell
Hoboken

}, month = {2015}, pages = {1901-1911}, abstract = {

Nitrate reductases (NR) belong to the DMSO reductase family of Mo-containing enzymes and perform key roles in the metabolism of the nitrogen cycle, reducing nitrate to nitrite. Due to variable cell location, structure and function, they have been divided into periplasmic (Nap), cytoplasmic, and membrane-bound (Nar) nitrate reductases. The first crystal structure obtained for a NR was that of the monomeric NapA from Desulfovibrio desulfuricans in 1999. Since then several new crystal structures were solved providing novel insights that led to the revision of the commonly accepted reaction mechanism for periplasmic nitrate reductases. The two crystal structures available for the NarGHI protein are from the same organism (Escherichia coli) and the combination with electrochemical and spectroscopic studies also lead to the proposal of a reaction mechanism for this group of enzymes. Here we present an overview on the current advances in structural and functional aspects of bacterial nitrate reductases, focusing on the mechanistic implications drawn from the crystallographic data.

}, keywords = {Biochemistry \& Molecular Biology, Biophysics, dehydrogenase, molybdenum enzymes, haemophilus-influenzae, catalytic, diheme cytochrome-c, crystal-structure, escherichia-coli, formate, enzymatic mechanism, marinobacter-hydrocarbonoclasticus 617, dimethyl-sulfoxide reductase,, mechanism, angstrom resolution, molybdenum enzymes, nitrogen cycle, DMSO reductase family, periplasmic, nitrate reductase, membrane-bound nitrate reductase, crystal structure,}, isbn = {0961-8368}, url = {://CCC:000368292000001http://www.wiley.com/WileyCDA/}, author = {Coelho, C. and Romao, M. J.} }