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Investigating the Structural, Spectroscopic, and Electrochemical Properties of [Fe{(EPiPr2)2N}2] (E = S, Se) and the Formation of Iron Selenides by Chemical Vapor Deposition

Levesanos, N., Liyanage, W. P. R., Ferentinos, E., Raptopoulos, G., Paraskevopoulou, P., Sanakis, Y., Choudhury, A., Stavropoulos, P., Nath, M., & Kyritsis, P. (2016) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201600833 · Cited by 15 · see citing works

Superoxide Processing

Miller, A. (2003) · Elsevier eBooks · doi:10.1016/b0-08-043748-6/08173-1 · Cited by 15 · see citing works

Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a ‘natural variant’

Todorović, S., Rodrigues, J. V., Pinto, A. F., Thomsen, C., Hildebrandt, P., Teixeira, M. S., & Murgida, D. H. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b815489a · Cited by 13 · see citing works

Fe–O versus O–O bond cleavage in reactive iron peroxide intermediates of superoxide reductase

Attia, A. A. A., Cioloboc, D., Lupan, A., & Silaghi-Dumitrescu, R. L. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0954-4 · Cited by 11 · see citing works

Superoxide Reductase: Different Interaction Modes with its Two Redox Partners

Almeida, R. M., Turano, P., Moura, I., Moura, J. J. G., & Pauleta, S. R. (2013) · ChemBioChem · doi:10.1002/cbic.201300196 · Cited by 11 · see citing works

Superoxide reductase activities of neelaredoxin and desulfoferrodoxin metalloproteins

Rusnak, F. M., Ascenso, C. S., Moura, I., & Moura, J. J. G. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49339-1 · Cited by 11 · see citing works

Peptide-based FeS4 complexes: the zinc ribbon fold is unsurpassed to stabilize both the FeII and FeIII states

Jacques, A., Latour, J., & Sénèque, O. (2014) · Dalton Transactions · doi:10.1039/c3dt53157k · Cited by 10 · see citing works

Electronic Structure of Tetrahedral, S = 2, [Fe{(EP i Pr 2 ) 2 N} 2 ], E = S, Se, Complexes: Investigation by High-Frequency and -Field Electron Paramagnetic Resonance, 57 Fe Mössbauer Spectroscopy, and Quantum Chemical Studies

Stoian, S. A., Moshari, M., Ferentinos, E., Grigoropoulos, A., Krzystek, J., Telser, J., & Kyritsis, P. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c00670 · Cited by 9 · see citing works

Nmr Structural Studies Of Iron-Sulfur Proteins

Goodfellow, B. J., & Macedo, A. L. (1999) · Annual reports on NMR spectroscopy · doi:10.1016/s0066-4103(08)60015-0 · Cited by 9 · see citing works

Rubredoxin

Meyer, J., & Moulis, J. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met135 · Cited by 9 · see citing works

Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site

Bonnot, F., Duval, S., Lombard, M., Valton, J., Houée‐Levin, C., & Nivière, V. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0788-5 · Cited by 8 · see citing works

Cloning, purification, crystallization and X-ray crystallographic analysis ofIgnicoccus hospitalisneelaredoxin

Pinho, F. G., Romão, C. V., Pinto, A. F., Saraiva, L. M., Huber, H., Matias, P. M., Teixeira, M. S., & Bandeiras, T. M. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309110012030 · Cited by 7 · see citing works

Iron–Sulfur Centers: New Roles for Ancient Metal Sites

Grazina, R., Pauleta, S. R., Moura, J. J. G., & Moura, I. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00308-9 · Cited by 7 · see citing works

Superoxide reductase fromGiardia intestinalis: structural characterization of the first SOR from a eukaryotic organism shows an iron centre that is highly sensitive to photoreduction

Sousa, C. M., Carpentier, P., Matias, P. M., Testa, F., Pinho, F., Sarti, P., Giuffrè, A., Bandeiras, T. M., & Romão, C. V. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004715015825 · Cited by 7 · see citing works

Oxygen and Anaerobes

Kurtz, D. M. J. (2003) · Springer eBooks · doi:10.1007/0-387-22731-8_10 · Cited by 7 · see citing works

Insights into the Structures of Superoxide Reductases from the Symbionts Ignicoccus hospitalis and Nanoarchaeum equitans

Romão, C. V., Matias, P. M., Sousa, C. M., Pinho, F. G., Pinto, A. F., Teixeira, M. S., & Bandeiras, T. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00334 · Cited by 6 · see citing works

Superoxide reductase from Desulfoarculus baarsii

Nivière, V., & Lombard, M. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49328-7 · Cited by 6 · see citing works

Nonheme iron proteins as an alternative system of antioxidant defense in the cells of strictly anaerobic microorganisms: A review

Brioukhanov, A. L. (2008) · Applied Biochemistry and Microbiology · doi:10.1134/s0003683808040017 · Cited by 5 · see citing works

Crystal Structure of Desulforedoxin fromDesulfovibrio gigasDetermined at 1.8 Å Resolution: A Novel Non-heme Iron Protein Structure

Archer, M., Huber, R., Tavares, P., Moura, I., Moura, J. J. G., Carrondo, M. A., Sieker, L. C., LeGall, J., & Romco, M. J. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0465 · Cited by 90 · see citing works

Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non‐heme iron proteins

Devreese, B. V., Tavares, P., Lampreia, J., Damme, N. V., LeGall, J., Moura, J. J. G., BEEUMEN, J. V., & Moura, I. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00364-x · Cited by 25 · see citing works

The solution structure of desulforedoxin, a simple iron-sulfur protein

Goodfellow, B. J., Tavares, P., Romão, M. J., Czaja, C., Rusnak, F. M., LeGall, J., Moura, I., & Moura, J. J. G. (1996) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050062 · Cited by 13 · see citing works

NMR solution structures of two mutants of desulforedoxin

Goodfellow, B. J., Rusnak, F. M., Moura, I., Ascenso, C. S., & Moura, J. J. G. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00458-0 · Cited by 1 · see citing works

On the two iron centers of desulfoferrodoxin

Verhagen, M. F. J. M., Voorhorst, W. G. B., Kolkman, J. A., WOLBERT, R. B. G., & Hagen, W. R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81599-u · Cited by 47 · see citing works