Publications

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Najmudin, S, Pauleta SR, Moura I, Romao MJ.  2010.  The 1.4 angstrom resolution structure of Paracoccus pantotrophus pseudoazurin. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 66:627-635. AbstractWebsite
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Najmudin, S, Bonifacio C, Duarte AG, Pauleta SR, Moura I, Moura JJG, Romao MJ.  2009.  Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas. (vol F65, pg 730, 2009). Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 65:856-856. AbstractWebsite
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Najmudin, S, Pinheiro BA, Prates JAM, Gilbert HJ, Romao MJ, Fontes CMGA.  2010.  Putting an N-terminal end to the Clostridium thermocellum xylanase Xyn10B story: Crystal structure of the CBM22-1-GH10 modules complexed with xylohexaose. Journal of Structural Biology. 172:353-362., Number 3 AbstractWebsite
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Najmudin, S, Bonifacio C, Duarte AG, Pualeta SR, Moura I, Moura JJG, Romao MJ.  2009.  Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 65:730-732. AbstractWebsite
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Najmudin, S, Pinheiro BA, Romao MJ, Prates JAM, Fontes CMGA.  2008.  Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-beta-D-xylanase 10B in complex with xylohexaose. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 64:715-718. AbstractWebsite
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Najmudin, S, Gonzalez PJ, Trincao J, Coelho C, Mukhopadhyay A, Cerqueira NMFSA, Romao CC, Moura I, Moura JJG, Brondino CD, Romao MJ.  2008.  Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum. Journal of Biological Inorganic Chemistry. 13:737-753., Number 5 AbstractWebsite
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Najmudin, S, Guerreiro C, Carvalho AL, Prates JAM, Correia MAS, Alves VD, Ferreira LMA, Romao MJ, Gilbert HJ, Bolam DN, Fontes C.  2006.  Xyloglucan is recognized by carbohydrate-binding modules that interact with beta-glucan chains. Journal of Biological Chemistry. 281:8815-8828., Number 13 AbstractWebsite
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Nóbrega, CS, Carvalho AL, Romão MJ, Pauleta SR.  2023.  Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase—Insights into the Catalytic Cycle of Bacterial Peroxidases. International Journal of Molecular Sciences. 24, Number 7 AbstractWebsite

Neisseria gonorrhoeae is an obligate human pathogenic bacterium responsible for gonorrhea, a sexually transmitted disease. The bacterial peroxidase, an enzyme present in the periplasm of this bacterium, detoxifies the cells against hydrogen peroxide and constitutes one of the primary defenses against exogenous and endogenous oxidative stress in this organism. The 38 kDa heterologously produced bacterial peroxidase was crystallized in the mixed-valence state, the active state, at pH 6.0, and the crystals were soaked with azide, producing the first azide-inhibited structure of this family of enzymes. The enzyme binds exogenous ligands such as cyanide and azide, which also inhibit the catalytic activity by coordinating the P heme iron, the active site, and competing with its substrate, hydrogen peroxide. The inhibition constants were estimated to be 0.4 ± 0.1 µM and 41 ± 5 mM for cyanide and azide, respectively. Imidazole also binds and inhibits the enzyme in a more complex mechanism by binding to P and E hemes, which changes the reduction potential of the latest heme. Based on the structures now reported, the catalytic cycle of bacterial peroxidases is revisited. The inhibition studies and the crystal structure of the inhibited enzyme comprise the first platform to search and develop inhibitors that target this enzyme as a possible new strategy against N. gonorrhoeae.