Publications

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1999
Dias, JM, Bursakov S, Carneiro C, Moura JJG, Moura I, Romao MJ.  1999.  Crystallization and preliminary X-ray analysis of a nitrate reductase from Desulfovibrio desulfuricans ATCC 27774. Acta Crystallographica Section D-Biological Crystallography. 55:877-879. AbstractWebsite
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Dias, JM, Than ME, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Moura JJG, Moura I, Romao MJ.  1999.  Crystallographic studies of a dissimilatory nitrate reductase and mechanistic implications. Journal of Inorganic Biochemistry. 74:113-113., Number 1-4 AbstractWebsite
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Teixeira, S, Dias JM, Carvalho AL, Bourenkov G, Bartunik H, Almendra MJ, Moura I, Moura JJG, Romao MJ.  1999.  Crystallographic studies on a tungsten-containning formate dehydrogenase from Desulfovibrio gigas. Journal of Inorganic Biochemistry. 74:89-89., Number 1-4 AbstractWebsite
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Cunha, CA, Romao MJ, Sadeghi SJ, Valetti F, Gilardi G, Soares CM.  1999.  Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes. Journal of Biological Inorganic Chemistry. 4:360-374., Number 3 AbstractWebsite
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Romao, MJ, Carvalho AL, Dias JM, Teixeira S, Bourenkov G, Bartunik H, Huber R, Maia L, Mira L.  1999.  Preliminary crystallographic studies of xanthine oxidase purified from rat liver. Journal of Inorganic Biochemistry. 74:281-281., Number 1-4 AbstractWebsite
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Archer, M, Carvalho AL, Teixeira S, Moura I, Moura JJG, Rusnak F, Romao MJ.  1999.  Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein. Protein Science. 8:1536-1545., Number 7 AbstractWebsite
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1998
Glatigny, A, Hof P, Romao MJ, Huber R, Scazzocchio C.  1998.  Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase. Journal of Molecular Biology. 278:431-438., Number 2 AbstractWebsite
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Romao, MJ, Huber R.  1998.  Structure and function of the xanthine-oxidase family of molybdenum enzymes. Metal Sites in Proteins and Models. 90:69-95. AbstractWebsite
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Voityuk, AA, Albert K, Romao MJ, Huber R, Rosch N.  1998.  Substrate oxidation in the active site of xanthine oxidase and related enzymes. A model density functional study. Inorganic Chemistry. 37:176-180., Number 2 AbstractWebsite
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1997
Varela, PF, Romero A, Sanz L, Romao MJ, Topfer-Petersen E, Calvete JJ.  1997.  The 2.4 angstrom resolution crystal structure of boar seminal plasma PSP-I/PSP-II: a zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture. Journal of Molecular Biology. 274:635-649., Number 4 AbstractWebsite
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Romao, MJ, Hubert R.  1997.  Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas. Biochemical Society Transactions. 25:755-757., Number 3 AbstractWebsite
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Romao, MJ, Kolln I, Dias JM, Carvalho AL, Romero A, Varela PF, Sanz L, Topfer-Petersen E, Calvete JJ.  1997.  Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 angstrom resolution: a bovine polypeptide of the spermadhesin family. Journal of Molecular Biology. 274:650-660., Number 4 AbstractWebsite
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Archer, M, Banci L, Dikaya E, Romao MJ.  1997.  Crystal structure of cytochrome c' from Rhodocyclus gelatinosus and comparison with other cytochromes c'. Journal of Biological Inorganic Chemistry. 2:611-622., Number 5 AbstractWebsite
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Romero, A, Romao MJ, Varela PF, Kolln I, Dias JM, Carvalho AL, Sanz L, TopferPetersen E, Calvete JJ.  1997.  The crystal structures of two spermadhesins reveal the CUB domain fold. Nature Structural Biology. 4:783-788., Number 10 AbstractWebsite
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Dias, JM, Carvalho AL, Kolln I, Calvete JJ, TopferPetersen E, Varela PF, Romero A, Urbanke C, Romao MJ.  1997.  Crystallization and preliminary x-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture. Protein Science. 6:725-727., Number 3 AbstractWebsite
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Voityuk, AA, Albert K, Kostlmeier S, Nasluzov VA, Neyman KM, Hof P, Huber R, Romao MJ, Rosch N.  1997.  Prediction of alternative structures of the molybdenum site in the xanthine oxidase-related aldehyde oxide reductase. Journal of the American Chemical Society. 119:3159-3160., Number 13 AbstractWebsite
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Romao, MJ, Knablein J, Huber R, Moura JJG.  1997.  Structure and function of molybdopterin containing enzymes. Progress in Biophysics & Molecular Biology. 68:121-144., Number 2-3 AbstractWebsite
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Romero, A, Varela PF, Romao MJ, Sanz L, TopferPetersen E, Calvete JJ.  1997.  The three-dimensional structure of mammalian spermadhesins determined by x-ray crystallography. European Journal of Cell Biology. 74:13-13. AbstractWebsite
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1996
Moura, JJG, Goodfellow BJ, Romao MJ, Rusnak F, Moura I.  1996.  Analysis, design and engineering of simple iron-sulfur proteins: Tales from rubredoxin and desulforedoxin. Comments on Inorganic Chemistry. 19:47-+., Number 1 AbstractWebsite
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Romero, A, Caldeira J, Legall J, Moura I, Moura JJG, Romao MJ.  1996.  Crystal structure of flavodoxin from Desulfovibrio desulfuricans ATCC 27774 in two oxidation states. European Journal of Biochemistry. 239:190-196., Number 1 AbstractWebsite
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Zajc, A, Romao MJ, Turk B, Huber R.  1996.  Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. Journal of Molecular Biology. 263:269-283., Number 2 AbstractWebsite
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Kiefersauer, R, Stetefeld J, GomisRuth FX, Romao MJ, Lottspeich F, Huber R.  1996.  Protein-crystal density by volume measurement and amino-acid analysis. Journal of Applied Crystallography. 29:311-317. AbstractWebsite
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Goodfellow, BJ, Tavares P, Romao MJ, Czaja C, Rusnak F, Legall J, Moura I, Moura JJG.  1996.  The solution structure of desulforedoxin, a simple iron-sulfur protein - An NMR study of the zinc derivative. Journal of Biological Inorganic Chemistry. 1:341-354., Number 4 AbstractWebsite
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Huber, R, Hof P, Duarte RO, Moura JJG, Moura I, Liu MY, Legall J, Hille R, Archer M, Romao MJ.  1996.  A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes. Proceedings of the National Academy of Sciences of the United States of America. 93:8846-8851., Number 17 AbstractWebsite
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