Publications

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2015

Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study, Gómez, M. C., Neuman N. I., Dalosto S. D., Gonzalez P. J., Moura J. J. G., Rizzi A. C., and Brondino C. D. , J Biol Inorg Chem, Volume 20, p.233–242, (2015)

Molybdenum and tungsten enzymes: from biology to chemistry and back, Moura, J. J. G., Bernhardt P. V., Maia L. B., and Gonzalez P. J. , J Biol Inorg Chem, Volume 20, p.181-182, (2015)

Molybdenum and tungsten-dependent formate dehydrogenases, Maia, L. B., Moura J. J. G., and Moura I. , J Biol Inorg Chem, Volume 20, p.287-309, (2015)

jbic-2015-20-287.pdf

Nitrite reductase activity of rat and human xanthine oxidase, xanthine dehydrogenase and aldehyde oxidase: evaluation of their contribution to the NO formation in vivo, Maia, L. B., Pereira V., Mira L., and Moura J. J. G. , Biochemistry, Volume 54, p.685-710, (2015)

Nitrite reduction by molybdoenzymes - A new class of nitric oxide-forming nitrite reductases, Maia, L. B., and Moura J. J. G. , J Biol Inorg Chem, Volume 20, p.403-433, (2015)

jbic-2015-20-403.pdf

Periplasmic nitrate reductase and formate dehydrogenase: similar molecular architectures with very different enzymatic activities, Cerqueira, N., Gonzalez P. J., Fernandes P. A., Moura J. J. G., and Ramos M. J. , Acc Chem Res, Volume 48, p.2875−2884, (2015)

Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase: redox dependence and insight into reactivity, Johnston, E. M., Dell'Acqua S., Pauleta S. R., Moura I., and Solomon E. I. , Chem Sci, Volume 6, p.5670-5679, (2015)

SERR spectroelectrochemical study of cytochrome cd1 nitrite reductase co-immobilized with physiological redox partner cytochrome c552 on biocompatible metal electrodes, Silveira, C. M., Quintas P. O., Moura I., Moura J. J. G., Hildebrandt P., Almeida M. G., and Todorovic S. , Plos One, Volume 10, p.e0129940, (2015)

2016

Detection of nitric oxide by electron paramagnetic resonance spectroscopy: spin-trapping with iron-dithiocarbamates, Maia, L. B., and Moura J. J. G. , Methods Mol Biol, Volume 1424, p.81-102, (2016) Website

Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study, Pedroso, H. A., Silveira C. M., Almeida R. M., Almeida A., Besson S., Moura I., Moura J. J. G., and Almeida M. G. , Biochim Biophys Acta, Volume 1857, p.1412-142104.279, (2016) Website

Orange protein from Desulfovibrio alaskensis G20: insights into the Mo-Cu cluster protein-assisted synthesis, Carepo, M. S., Carreira C., Grazina R., Zakrzewska M. E., Dolla A., Aubert C., Pauleta S. R., Moura J. J. G., and Moura I. , J Biol Inorg Chem, Volume 21, p.53-62, (2016)

Predicting Protein-Protein Interactions Using BiGGER: Case Studies, Almeida, R. M., Dell'Acqua S., Krippahl L., Moura J. J. G., and Pauleta S. R. , Molecules, Volume 21, p.1037, (2016) Website

Proteins dominate in the surface layers formed on materials exposed to extracellular polymeric substances from bacterial cultures, Yang, Y., Wikieł A. J., Dall'agnol L. T., Eloy P., Genet M. J., Moura J. J. G., Sand W., Dupont-Gillain C. C., and Rouxhet P. G. , Biofouling, Volume 32, p.95-108, (2016)

Reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study, Maia, L. B., Fonseca L., Moura I., and Moura J. J. G. , J Am Chem Soc, Volume 138, p.8834-8846, (2016) Website

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly, Carvalho, R., Almeida R., Moura J. J. G., Lourenço N., Fonseca L., and Cordas C. M. , Chemistry Select, Volume 1, p.6546–6552, (2016) Website

The small iron-sulfur protein from the ORP operon binds a [2Fe-2S] cluster, Maiti, B. K., Moura I., Moura J. J. G., and Pauleta S. R. , Biochim Biophys Acta, Volume 1857, p.1422-1429, (2016) Website

Synthesis of WO3 nanoparticles for biosensing applications, Santos, L., Silveira C. M., Elangovan E., Neto J. P., Nunes D., Pereira L., Martins R., Viegas J., Moura J. J. G., Todorovic S., Almeida M. G., and Fortunato E. M. , Sensors and Actuators B: Chemical, Volume 223, p.186-194, (2016)

2017

A bird’s-eye view of denitrification in relation to the nitrogen cycle, Moura, I., Maia L. B., Pauleta S. R., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., Cambridge, p.1-10, (2017) n_cycle-rsc_book-denitrification-chap_1.pdf

The catalytic cycle of nitrous oxide reductase - The enzyme that catalyzes the last step of denitrification, Carreira, C., Pauleta S. R., and Moura I. , J Inorg Biochem, Volume 177, p.423-434, (2017)

Comparative electrochemical behavior of cytochrome c on aqueous solutions containing choline-based room temperature ionic liquids, Matias, S. C., Lourenço N. M. T., Fonseca J. P., and Cordas C. M. , ChemistrySelect, Volume 2, p.8701–8705, (2017) Website

Electron transfer and molecular recognition in denitrification and nitrate dissimilatory pathways, Almeida, R. M., Dell'Acqua S., Moura I., Pauleta S. R., and Moura J. J. G. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., p.252-286, (2017)

EPR spectroscopy on mononuclear molybdenum-containing enzymes, Maia, L. B., Moura I., and Moura J. J. G. , Future Directions in Metalloprotein and Metalloenzyme Research, Biological Magnetic Resonance, Vol. 33 (ISBN: 978-3-319-59100-1), Cham, p.55-101, (2017) Abstract

The biological relevance of molybdenum was demonstrated in the early 1950s-1960s, by Bray, Beinert, Lowe, Massey, Palmer, Ehrenberg, Pettersson, Vänngård, Hanson and others, with ground-breaking studies performed, precisely, by electron paramagnetic resonance (EPR) spectroscopy. Those earlier studies, aimed to investigate the mammalian xanthine oxidase and avian sulfite oxidase enzymes, demonstrated the surprising biological reduction of molybdenum to the paramagnetic Mo⁵⁺. Since then, EPR spectroscopy, alongside with other spectroscopic methods and X-ray crystallography, has contributed to our present detailed knowledge about the active site structures, catalytic mechanisms and structure/activity relationships of the molybdenum-containing enzymes.
This Chapter will provide a perspective on the contribution that EPR spectroscopy has made to some selected systems. After a brief overview on molybdoenzymes, the Chapter will be focused on the EPR studies of mammalian xanthine oxidase, with a brief account on the prokaryotic aldehyde oxidoreductase, nicotinate dehydrogenase and carbon monoxide dehydrogenase, vertebrate sulfite oxidase, and prokaryotic formate dehydrogenases and nitrate reductases.

Insights into nitrous oxide reductase, Pauleta, S. R., Carreira C., and Moura I. , Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2)., p.141-169, (2017)

Insights into the molybdenum/copper heterometallic cluster assembly in the orange protein: probing intermolecular interactions with an artificial metal-binding ATCUN tag, Maiti, B. K., Almeida R. M., Maia L. B., Moura I., and Moura J. J. G. , Inorg Chem, Volume 56, p.8900-8911, (2017) Website

Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus, Ramos, S., Almeida R. M., Cordas C. M., Moura J. J. G., Pauleta S. R., and Moura I. , J Inorg Biochem, Volume 177, p.402-411, (2017)