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
Abstractn/a
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
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Romao, MJ, Barata BAS, Archer M, Lobeck K, Moura I, Carrondo MA, Legall J, Lottspeich F, Huber R, Moura JJG.
1993.
SUBUNIT COMPOSITION, CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF THE DESULFOVIBRIO-GIGAS ALDEHYDE OXIDOREDUCTASE CONTAINING MOLYBDENUM AND 2FE-2S CENTERS. European Journal of Biochemistry. 215:729-732., Number 3
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Kryshtafovych, A, Albrecht R, Baslé A, Bule P, Caputo AT, Carvalho AL, Chao KL, Diskin R, Fidelis K, Fontes CMGA, Fredslund F, Gilbert HJ, Goulding CW, Hartmann MD, Hayes CS, Herzberg O, Hill JC, Joachimiak A, Kohring G-W, Koning RI, {Lo Leggio} L, Mangiagalli M, Michalska K, Moult J, Najmudin S, Nardini M, Nardone V, Ndeh D, Nguyen TH, Pintacuda G, Postel S, van Raaij MJ, Roversi P, Shimon A, Singh AK, Sundberg EJ, Tars K, Zitzmann N, Schwede T.
2017.
Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016), oct. Proteins: Structure, Function, and Bioinformatics.
AbstractThe functional and biological significance of the selected CASP12 targets are described by the authors of the structures. The crystallographers discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP12 experiment. This article is protected by copyright. All rights reserved.
Hussain, A, Semeano ATS, Palma SICJ, Pina AS, Almeida J, Medrado BF, Pádua ACCS, Carvalho AL, Dionísio M, Li RWC, Gamboa H, Ulijn RV, Gruber J, Roque ACA.
2017.
Tunable Gas Sensing Gels by Cooperative Assembly. Advanced Functional Materials. 27:1700803–n/a., Number 27
AbstractThe cooperative assembly of biopolymers and small molecules can yield functional materials with precisely tunable properties. Here, the fabrication, characterization, and use of multicomponent hybrid gels as selective gas sensors are reported. The gels are composed of liquid crystal droplets self-assembled in the presence of ionic liquids, which further coassemble with biopolymers to form stable matrices. Each individual component can be varied and acts cooperatively to tune gels' structure and function. The unique molecular environment in hybrid gels is explored for supramolecular recognition of volatile compounds. Gels with distinct compositions are used as optical and electrical gas sensors, yielding a combinatorial response conceptually mimicking olfactory biological systems, and tested to distinguish volatile organic compounds and to quantify ethanol in automotive fuel. The gel response is rapid, reversible, and reproducible. These robust, versatile, modular, pliant electro-optical soft materials possess new possibilities in sensing triggered by chemical and physical stimuli.
Correia, MAS, Otrelo-Cardoso AR, Schwuchow V, {Sigfridsson Clauss} KGV, Haumann M, Romão MJ, Leimkühler S, Santos-Silva T.
2016.
{The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes}, oct. ACS Chemical Biology. 11:2923–2935., Number 10
AbstractThe xanthine oxidase (XO) family comprises molybdenum-dependent enzymes that usually form homodimers (or dimers of heterodimers/trimers) organized in three domains that harbor two [2Fe-2S] clusters, one FAD, and a Mo cofactor. In this work, we crystallized an unusual member of the family, the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli. This is the first example of an E. coli protein containing a molybdopterin-cytosine-dinucleotide cofactor and is the only heterotrimer of the XO family so far structurally characterized. The crystal structure revealed the presence of an unexpected [4Fe-4S] cluster, anchored to an additional 40 residues subdomain. According to phylogenetic analysis, proteins containing this cluster are widely spread in many bacteria phyla, putatively through repeated gene transfer events. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (PaoC-R440) making a direct interaction with PaoC-E692, which acts as a base catalyst. In order to understand the importance of R440, kinetic assays were carried out, and the crystal structure of the PaoC-R440H variant was also determined.