Biochemistry, Stereochemistry, Active site, Enzyme and Xanthine oxidase are her primary areas of study. Biochemistry is frequently linked to Biophysics in her study. Her work deals with themes such as Multiple isomorphous replacement, Reductase, Crystal structure and Molybdopterin, which intersect with Stereochemistry.
Her research in Enzyme intersects with topics in Schiff base and Binding site. Her Xanthine oxidase research incorporates themes from Cofactor and Xanthine. As part of the same scientific family, she usually focuses on Cofactor, concentrating on Molybdenum and intersecting with Crystallography.
Her scientific interests lie mostly in Stereochemistry, Crystallography, Biochemistry, Crystal structure and Enzyme. Her Stereochemistry research includes elements of Molybdenum, Molybdopterin, Oxidoreductase, Heme and Active site. Her research integrates issues of Formate dehydrogenase and Pterin in her study of Molybdopterin.
Her studies deal with areas such as Substrate, Redox and Cofactor as well as Active site. The study incorporates disciplines such as Cytochrome, Crystallization, Molecule and Dimer in addition to Crystallography. Her Enzyme research is multidisciplinary, relying on both Binding site and Escherichia coli.
Her primary scientific interests are in Biochemistry, Aldehyde oxidase, Stereochemistry, Enzyme and Active site. Her Aldehyde oxidase research integrates issues from Xanthine dehydrogenase, Isozyme and Phthalazine. Maria João Romão focuses mostly in the field of Stereochemistry, narrowing it down to matters related to Crystal structure and, in some cases, DNA, Biophysics and Mutant.
Her study in Enzyme is interdisciplinary in nature, drawing from both Protein structure and Gene isoform, Gene, Escherichia coli. The Protein structure study combines topics in areas such as Crystallography, Protein engineering, Conformational entropy and Nuclear magnetic resonance spectroscopy. Her Active site study combines topics in areas such as Plasma protein binding, Oxidoreductase, Substrate, Electron transfer and Electron acceptor.
The scientist’s investigation covers issues in Biochemistry, Enzyme, Aldehyde oxidase, Stereochemistry and Drug metabolism. Her work on Active site, Amino acid, Dehydrogenase and Cell wall as part of general Biochemistry study is frequently connected to Chitin, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. Non-competitive inhibition and Plasma protein binding is closely connected to Substrate in her research, which is encompassed under the umbrella topic of Active site.
Her study in Xanthine oxidase and Oxidoreductase falls under the purview of Enzyme. Maria João Romão combines subjects such as Isozyme, Xenobiotic and Gene with her study of Aldehyde oxidase. She is interested in Isocyanide, which is a field of Stereochemistry.
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Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
Maria J. Romão;Margarida Archer;Isabel Moura;José J. G. Moura.
Science (1995)
Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods.
João M. Dias;Manuel E. Than;Andreas Humm;Robert Huber.
Structure (1999)
A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes
Robert Huber;Peter Hof;Rui O. Duarte;Jose J. G. Moura.
Proceedings of the National Academy of Sciences of the United States of America (1996)
Cellulosome assembly revealed by the crystal structure of the cohesin–dockerin complex
Ana L. Carvalho;Fernando M. V. Dias;José A. M. Prates;Tibor Nagy.
Proceedings of the National Academy of Sciences of the United States of America (2003)
Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology
Enrico Garattini;Ralf Mendel;Maria João Romão;Richard Wright.
Biochemical Journal (2003)
Nickel(0)-induzierte CC-verknüpfung zwischen kohlendioxid und alkinen sowie alkenen
H. Hoberg;D. Schaefer;G. Burkhart;C. Krüger.
Journal of Organometallic Chemistry (1984)
Corm-3 Reactivity Toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl-Lysozyme Complex.
Teresa Sacadura Santos-silva;Abhik Mukhopadhyay;João D. Seixas;Gonçalo J L Bernardes.
Journal of the American Chemical Society (2011)
Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas
Hans Raaijmakers;Sofia Macieira;Sofia Macieira;João M Dias;Susana Teixeira.
Structure (2002)
The crystal structures of two spermadhesins reveal the CUB domain fold
Antonio Romero;Maria J. Romão;Paloma F. Varela;Ingo Kölln.
Nature Structural & Molecular Biology (1997)
Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases
José J. G. Moura;Carlos D. Brondino;Carlos D. Brondino;José Trincão;Maria João Romão.
Journal of Biological Inorganic Chemistry (2004)
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