Publications

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Almeida, MG, Macieira S, Goncalves LL, Huber R, Cunha CA, Romao MJ, Costa C, Lampreia J, Moura JJG, Moura I.  2003.  The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774 - Re-evaluation of the spectroscopic data and redox properties. European Journal of Biochemistry. 270:3904-3915., Number 19 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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Archer, M, Huber R, Tavares P, Moura I, Moura JJG, Carrondo MA, Sieker LC, Legall J, Romao MJ.  1995.  CRYSTAL-STRUCTURE OF DESULFOREDOXIN FROM DESULFOVIBRIO-GIGAS DETERMINED AT 1.8 ANGSTROM RESOLUTION - A NOVEL NONHEME IRON PROTEIN-STRUCTURE. Journal of Molecular Biology. 251:690-702., Number 5 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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Aveiro, SS, Freire F, Clayton J, Cameloc M, Carvalho AL, Ferreira GC, Romao MJ, Macedo AL, Goodfellow BJ.  2012.  Structural studies of the p22HBP/SOUL family of heme-binding proteins. Febs Journal. 279:458-458. AbstractWebsite
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Boer, DR, Thapper A, Brondino CD, Romao MJ, Moura JJG.  2004.  X-ray crystal structure and EPR spectra of "arsenite-inhibited" Desulfovibrio gigas aldehyde dehydrogenase: A member of the xanthine oxidase family. Journal of the American Chemical Society. 126:8614-8615., Number 28 AbstractWebsite
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Boer, DR, Muller A, Fetzner S, Lowe DJ, Romao MJ.  2005.  On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 61:137-140. AbstractWebsite
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Bonifacio, C, Cunha CA, Muller A, Timoteo CG, Dias JM, Moura I, Romao MJ.  2003.  Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri. Acta Crystallographica Section D-Biological Crystallography. 59:345-347. AbstractWebsite
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Branco, PS, Peixoto D, Figueiredo M, Malta G, Roma-Rodrigues C, Batista PV, Fernandes AR, Barroso S, Carvalho AL, Afonso CAM, Ferreira LM.  2018.  Synthesis, cytotoxicity evaluation in human cell lines and in vitro DNA interaction of a hetero arylidene-9(10H)-anthrone. European Journal of Organic Chemistry. :n/a–n/a. AbstractWebsite

A new and never yet reported hetero arylidene-9(10H)-anthrone structure (4) was unexpectedly isolated on reaction of 1,2-dimethyl-3-ethylimidazolium iodide (2) and 9-anthracenecarboxaldehyde (3) under basic conditions. Its structure was unequivocally attributed by X-ray crystallography. No cytotoxicity in human healthy fibroblasts and in two different cancer cell lines was observed indicating its applicability in biological systems. Compound 4 interacts with CT-DNA by intercalation between the adjacent base pairs of DNA with a high binding affinity (Kb = 2.0(± 0.20) x 105 M-1) which is 10x higher than that described for doxorubicin (Kb = 3.2 (±0.23) × 104 M-1). Furthermore, compound 4 quenches the fluorescence emission of GelRed-CT-DNA system with a quenching constant (KSV) of 3.3(±0.3) x 103 M-1 calculated by the Stern-Volmer equation.

Bras, JLA, Cartmell A, Carvalho ALM, Verze G, Bayer EA, Vazana Y, Correia MAS, Prates JAM, Ratnaparkhe S, Boraston AB, Romao MJ, Fontes CMGA, Gilbert HJ.  2011.  Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis. Proceedings of the National Academy of Sciences of the United States of America. 108:5237-5242., Number 13 AbstractWebsite
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Bras, JLA, Carvalho AL, Viegas A, Najmudin S, Alves VD, Prates JAM, Ferreira LMA, Romao MJ, Gilbert HJ, Fontes CMGA.  2012.  ESCHERICHIA COLI EXPRESSION, PURIFICATION, CRYSTALLIZATION, AND STRUCTURE DETERMINATION OF BACTERIAL COHESIN-DOCKERIN COMPLEXES. Cellulases. 510(Gilbert, H. J., Ed.).:395-415. Abstract
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Bras, JLA, Correia MAS, Romao MJ, Prates JAM, Fontes CMGA, Najmudin S.  2011.  Purification, crystallization and preliminary X-ray characterization of the pentamodular arabinoxylanase CtXyl5A from Clostridium thermocellum. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 67:833-836. AbstractWebsite
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Bras, JLA, Alves VD, Carvalho AL, Najmudin S, Prates JAM, Ferreira LMA, Bolam DN, Romao MJ, Gilbert HJ, Fontes CMGA.  2012.  Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode. Journal of Biological Chemistry. 287:44394-44405., Number 53 AbstractWebsite
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Brás, JLA, Pinheiro BA, Cameron K, Cuskin F, Viegas A, Najmudin S, Bule P, Pires VMR, Romão MJ, Bayer EA, Spencer HL, Smith S, Gilbert HJ, Alves VD, Carvalho AL, Fontes CMGA.  2016.  Diverse specificity of cellulosome attachment to the bacterial cell surface, dec. Scientific Reports. 6:38292.: The Author(s) AbstractWebsite

During the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.

Brondino, CD, Romao MJ, Moura I, Moura JJG.  2006.  Molybdenum and tungsten enzymes: the xanthine oxidase family. Current Opinion in Chemical Biology. 10:109-114., Number 2 AbstractWebsite
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Brondino, CD, Rivas MG, Romao MJ, Moura JJG, Moura I.  2006.  Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria. Accounts of Chemical Research. 39:788-796., Number 10 AbstractWebsite
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Brondino, CD, Rivas MG, Romao MJ, Moura JJG, Moura I.  2007.  Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria (vol 39, pg 793, 2006). Accounts of Chemical Research. 40:231-231., Number 3 AbstractWebsite
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Bule, P, Alves VD, Israeli-Ruimy V, Carvalho AL, Ferreira LMA, Smith SP, Gilbert HJ, Najmudin S, Bayer EA, Fontes CMGA.  2017.  Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes, 2017. Scientific Reports. 7:759. AbstractWebsite

Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens’ cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.

Bule, P, Pires VMR, Alves VD, Carvalho AL, Prates JAM, Ferreira LMA, Smith SP, Gilbert HJ, Noach I, Bayer EA, Najmudin S, Fontes CMGA.  2018.  Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction, 2018. Scientific Reports. 8(1):6987. AbstractWebsite

Cellulosomes are highly sophisticated molecular nanomachines that participate in the deconstruction of complex polysaccharides, notably cellulose and hemicellulose. Cellulosomal assembly is orchestrated by the interaction of enzyme-borne dockerin (Doc) modules to tandem cohesin (Coh) modules of a non-catalytic primary scaffoldin. In some cases, as exemplified by the cellulosome of the major cellulolytic ruminal bacterium Ruminococcus flavefaciens, primary scaffoldins bind to adaptor scaffoldins that further interact with the cell surface via anchoring scaffoldins, thereby increasing cellulosome complexity. Here we elucidate the structure of the unique Doc of R. flavefaciens FD-1 primary scaffoldin ScaA, bound to Coh 5 of the adaptor scaffoldin ScaB. The RfCohScaB5-DocScaA complex has an elliptical architecture similar to previously described complexes from a variety of ecological niches. ScaA Doc presents a single-binding mode, analogous to that described for the other two Coh-Doc specificities required for cellulosome assembly in R. flavefaciens. The exclusive reliance on a single-mode of Coh recognition contrasts with the majority of cellulosomes from other bacterial species described to date, where Docs contain two similar Coh-binding interfaces promoting a dual-binding mode. The discrete Coh-Doc interactions observed in ruminal cellulosomes suggest an adaptation to the exquisite properties of the rumen environment.

Bursakov, SA, Brondino C, Dias JM, Carneiro C, Caldeira J, Duarte RO, Romao MJ, Moura I, Moura JJG.  1999.  Cross immunological reactions and spectroscopy study within nitrate reductase and other mononuclear Mo containing enzymes of the sulfate reducing bacteria. Journal of Inorganic Biochemistry. 74:86-86., Number 1-4 AbstractWebsite
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Capodicasa, C, Chiani P, Bromuro C, De Bernardis F, Catellani M, Palma AS, Liu Y, Feizi T, Cassone A, Benvenuto E, Torosantucci A.  2011.  Plant production of anti-beta-glucan antibodies for immunotherapy of fungal infections in humans. Plant Biotechnology Journal. 9:776-787., Number 7 AbstractWebsite
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Carvalho, AL, Dias JM, Sanz L, Romero A, Calvete JJ, Romao MJ.  2001.  Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma. Acta Crystallographica Section D-Biological Crystallography. 57:1180-1183. AbstractWebsite
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Carvalho, AL, Dias FMV, Nagy T, Prates JAM, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LMA, Romao MJ, Fontes CMGA, Gilbert HJ.  2007.  Evidence for a dual binding mode of dockerin modules to cohesins. Proceedings of the National Academy of Sciences of the United States of America. 104:3089-3094., Number 9 AbstractWebsite
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Carvalho, AL, Goyal A, Prates JAM, Bolam DN, Gilbert HJ, Pires VMR, Ferreira LMA, Planas A, Romao MJ, Fontes C.  2004.  The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site. Journal of Biological Chemistry. 279:34785-34793., Number 33 AbstractWebsite
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Carvalho, AL, Pires VMR, Gloster TM, Turkenburg JP, Prates JAM, Ferreira LMA, Romao MJ, Davies GJ, Fontes C, Gilbert HJ.  2005.  Insights into the structural determinants of cohesin dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA. Journal of Molecular Biology. 349:909-915., Number 5 AbstractWebsite
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