Ribeiro J.V., Lucas T.G., Bross P., Gomes C.M., Henriques B.J.
Biochimica et Biophysica Acta - Proteins and Proteomics (2020) 1868(1)
113. Identification of temperature-sensitive mutations and characterization of thermolabile RNase II variants
Reis, F.P., Barria, C., Gomez-Puertas, P., Gomes, C.M., Arraiano, C.M.
FEBS Lett (2019) 593, 352-360
https://doi.org/10.1002/1873-3468.13313
112. Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution
Moreira, G.G., Cristovao, J.S., Torres, V.M., Carapeto, A.P., Rodrigues, M.S., Landrieu, I., Cordeiro, C., Gomes, C.M.
Int J Mol Sci (2019) 20,
111. Molecular and Clinical Investigations on Portuguese Patients with Multiple acyl-CoA Dehydrogenase Deficiency
Henriques, B.J., Lucas, T.G., Martins, E., Gaspar, A., Bandeira, A., Nogueira, C., Brandao, O., Rocha, H., Vilarinho, L., Gomes, C.M.
Current molecular medicine (2019) 19, 487-493
110. Distribution and Relative Abundance of S100 Proteins in the Brain of the APP23 Alzheimer’s Disease Model Mice
Hagmeyer, S., Romão, M.A., Cristóvão, J.S., Vilella, A., Zoli, M., Gomes, C.M., Grabrucker, A.M.
Frontiers in Neuroscience (2019) 13,
109. S100 Proteins in Alzheimer’s Disease
Cristóvão, J.S., Gomes, C.M.
Frontiers in Neuroscience (2019) 13,
108. Impaired oligodendrogenesis and myelination by elevated S100B levels during neurodevelopment.
Santos, G., Barateiro, A., Gomes, C.M., Brites, D., Fernandes, A.
Neuropharmacology (2018) 129, 69-83
107. Zinc binding to S100B affords regulation of trace metal homeostasis and excitotoxicity in the brain
Hagmeyer, S., Cristóvão, J.S., Mulvihill, J.J., Boeckers, T.M., Gomes, C.M., Grabrucker, A.M.
Frontiers in Molecular Neuroscience (2018) 10,
106. The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation
Cristóvão, J.S., Morris, V.K., Cardoso, I., Leal, S.S., Martínez, J., Botelho, H.M., Göbl, C., David, R., Kierdorf, K., Alemi, M., Madl. T., Fritz, G., Reif, B., Gomes, C.M.
Science Advances (2018) 4, eaaq1702
105. Synthesis and effects of flavonoid structure variation on amyloid-β aggregation
Matos, A.M., Cristóvão, J.S., Yashunsky, D.V., Nifantiev, N.E., Viana, A.S., Gomes, C.M., Rauter, A.P.
Pure and Applied Chemistry (2017) 89,
https://doi.org/https://doi.org/10.1515/pac-2017-0201
104 Characterization of plasma labile heme in hemolytic conditions
Gouveia, Z., Carlos, A.R., Yuan, X., Aires-da-Silva, F., Stocker, R., Maghzal, G.J., Leal, S.S., Gomes, C.M., Todorovic, S., Iranzo, O., Ramos, S., Santos, A.C., Hamza, I., Gonçalves, J., Soares, M.P.
FEBS Journal (2017) 284, 3278-3301
https://doi.org/https://doi.org/10.1111/febs.14192
103. Evidence for synergistic action of transthyretin and IGF-I over the IGF-I receptor
Vieira, M., Leal, S.S., Gomes, C.M., Saraiva, M.J.
Biochim Biophys Acta (2016) 1862, 797-804
https://doi.org/10.1016/j.bbadis.2016.01.008
102. Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Abeta Peptide and O2
Reybier, K., Ayala, S., Alies, B., Rodrigues, J.V., Bustos Rodriguez, S., La Penna, G., Collin, F., Gomes, C.M., Hureau, C., Faller, P.
Angewandte Chemie (International ed. in English) (2016) 55, 1085-1089
https://doi.org/10.1002/anie.201508597
101. Therapeutic Approaches Using Riboflavin in Mitochondrial Energy Metabolism Disorders
Henriques, B.J., Lucas, T.G., Gomes, C.M.
Current drug targets (2016) 17, 1527-1534
100. Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer's Disease
Cristovao, J.S., Santos, R., Gomes, C.M.
Oxid Med Cell Longev (2016) 2016, 9812178
https://doi.org/10.1155/2016/9812178
99. Metallothioneins in Prion- and Amyloid-Related Diseases
Adam, P., Krizkova, S., Heger, Z., Babula, P., Pekarik, V., Vaculovicoa, M., Gomes, C.M., Kizek, R., Adam, V.
Journal of Alzheimer's disease : JAD (2016) 51, 637-656
https://doi.org/10.3233/JAD-150984
98. Calcium dysregulation links ALS defective proteins and motor neuron selective vulnerability
Leal, S.S., Gomes, C.M.
Frontiers in cellular neuroscience (2015) 9, 225
https://doi.org/10.3389/fncel.2015.00225
97. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation
Leal, S.S., Cristovao, J.S., Biesemeier, A., Cardoso, I., Gomes, C.M.
Metallomics (2015) 7, 333-346
https://doi.org/10.1039/c4mt00278d
96. Calcium binding to gatekeeper residues flanking aggregation-prone segments underlies non-fibrillar amyloid traits in superoxide dismutase 1 (SOD1)
Estacio, S.G., Leal, S.S., Cristovao, J.S., Faisca, P.F., Gomes, C.M.
Biochim Biophys Acta (2015) 1854, 118-126
https://doi.org/10.1016/j.bbapap.2014.11.005
95. On the hunt for truly biocompatible ionic liquids for lipase-catalyzed reactions
Deive, F.J., Ruivo, D., Rodrigues, J.V., Gomes, C.M., Sanroman, M.A., Rebelo, L.P.N., Esperanca, J.M.S.S., Rodriguez, A.
RSC Advances (2015) 5, 3386-3389
https://doi.org/10.1039/c4ra15021j
D
94. Structural-functional evaluation of ionic liquid libraries for the design of co-solvents in lipase-catalysed reactions
Rodrigues, J.V., Ruivo, D., Rodriguez, A., Deive, F.J., Esperanca, J.M.S.S., Marrucho, I.M., Gomes, C.M., Rebelo, L.P.N.
Green Chemistry (2014),
https://doi.org/10.1039/c4gc01329h
93. Ethylmalonic Encephalopathy ETHE1 R163W/R163Q Mutations Alter Protein Stability and Redox Properties of the Iron Centre
Henriques, B.J., Lucas, T.G., Rodrigues, J.V., Frederiksen, J.H., Teixeira, M.S., Tiranti, V., Bross, P., Gomes, C.M.
PloS one (2014) 9, e107157
https://doi.org/10.1371/journal.pone.0107157
92. A Conserved Cysteine Residue of Bacillus subtilis SpoIIIJ Is Important for Endospore Development
Corte, L., Valente, F., Serrano, M., Gomes, C.M., Moran, C.P., Jr., Henriques, A.O.
PloS one (2014) 9, e99811
https://doi.org/10.1371/journal.pone.0099811
91. Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform
Correia, A.R., Naik, S., Fisher, M.T., Gomes, C.M.
Biomolecules (2014) 4, 956-979
https://doi.org/10.3390/biom4040956
90. Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1
Sá-Moura, B., Simões, A.M., Fraga, J., Fernandes, H., Abreu, I.A., Botelho, H.M., Gomes, C.M., Marques, A.J., Dohmen, R.J., Ramos, P.C., Macedo-Ribeiro, S.
Comput Struct Biotechnol J (2013) 7, e201304006
https://doi.org/10.5936/csbj.201304006
89. Calcium Ions Promote Superoxide Dismutase 1 (SOD1) Aggregation into Non-fibrillar Amyloid: A LINK TO TOXIC EFFECTS OF CALCIUM OVERLOAD IN AMYOTROPHIC LATERAL SCLEROSIS (ALS)?
Leal, S.S., Cardoso, I., Valentine, J.S., Gomes, C.M.
J Biol Chem (2013) 288, 25219-25228
https://doi.org/10.1074/jbc.M113.470740
88. Neurodegeneration in Friedreich's Ataxia: From Defective Frataxin to Oxidative Stress
Gomes, C.M., Santos, R.
Oxid Med Cell Longev (2013) 2013, 487534
https://doi.org/10.1155/2013/487534
87. Revertants, Low Temperature, and Correctors Reveal the Mechanism of F508del-CFTR Rescue by VX-809 and Suggest Multiple Agents for Full Correction
Farinha, C.M., King-Underwood, J., Sousa, M., Correia, A.R., Henriques, B.J., Roxo-Rosa, M., Da Paula, A.C., Williams, J., Hirst, S., Gomes, C.M., Amaral, M.D.
Chemistry & Biology (2013) 20, 943-955
https://doi.org/10.1016/j.chembiol.2013.06.004
86. Small molecules present in the cerebrospinal fluid metabolome influence superoxide dismutase 1 aggregation
Cristovao, J.S., Leal, S.S., Cardoso, I., Gomes, C.M.
Int J Mol Sci (2013) 14, 19128-19145
https://doi.org/10.3390/ijms140919128
85. Intrinsically Disordered and Aggregation Prone Regions Underlie beta-Aggregation in S100 Proteins
Carvalho, S.B., Botelho, H.M., Leal, S.S., Cardoso, I., Fritz, G., Gomes, C.M.
PloS one (2013) 8, e76629
https://doi.org/10.1371/journal.pone.0076629
84. The sulfur oxygenase reductase from the mesophilic bacterium Halothiobacillus neapolitanus is a highly active thermozyme
Veith, A., Botelho, H.M., Kindinger, F., Gomes, C.M., Kletzin, A.
Journal of bacteriology (2012) 194, 677-685
https://doi.org/10.1128/JB.06531-11
83. Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors
Silva, M.A., Lucas, T.G., Salgueiro, C.A., Gomes, C.M.
PloS one (2012) 7, e46328
https://doi.org/10.1371/journal.pone.0046328
82. Cofactors and metabolites as protein folding helpers in metabolic diseases
Rodrigues, J.V., Henriques, B.J., Lucas, T.G., Gomes, C.M.
Curr Top Med Chem (2012) 12, 2546-2559
https://doi.org/http://dx.doi.org/10.2174/1568026611212220009
81. Mechanism of superoxide and hydrogen peroxide generation by human electron-transfer flavoprotein and pathological variants
Rodrigues, J.V., Gomes, C.M.
Free radical biology & medicine (2012) 53, 12-19
https://doi.org/10.1016/j.freeradbiomed.2012.04.016
80. Metal ions as modulators of protein conformation and misfolding in neurodegeneration
Leal, S.S., Botelho, H.M., Gomes, C.M.
Coordination Chemistry Reviews (2012) 256, 2253-2270
https://doi.org/10.1016/j.ccr.2012.04.004
79. Protein misfolding in disease and small molecule therapies
Gomes, C.M.
Curr Top Med Chem (2012) 12, 2460-2469
https://doi.org/http://dx.doi.org/10.2174/1568026611212220002
78. S100A6 Amyloid Fibril Formation Is Calcium-modulated and Enhances Superoxide Dismutase-1 (SOD1) Aggregation
Botelho, H.M., Leal, S.S., Cardoso, I., Yanamandra, K., Morozova-Roche, L.A., Fritz, G., Gomes, C.M.
J Biol Chem (2012) 287, 42233-42242
https://doi.org/10.1074/jbc.M112.396416
77. Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila
Alves, E., Henriques, B.J., Rodrigues, J.V., Prudencio, P., Rocha, H., Vilarinho, L., Martinho, R.G., Gomes, C.M.
Biochim Biophys Acta (2012) 1822, 1284-1292
https://doi.org/10.1016/j.bbadis.2012.05.003
76. Protein stability in an ionic liquid milieu: on the use of differential scanning fluorimetry
Rodrigues, J.V., Prosinecki, V., Marrucho, I., Rebelo, L.P., Gomes, C.M.
Physical chemistry chemical physics : PCCP (2011) 13, 13614-13616
https://doi.org/10.1039/c1cp21187k
75. Cofactors and metabolites as potential stabilizers of mitochondrial acyl-CoA dehydrogenases
Lucas, T.G., Henriques, B.J., Rodrigues, J.V., Bross, P., Gregersen, N., Gomes, C.M.
Biochim Biophys Acta (2011) 1812, 1658-1663
https://doi.org/10.1016/j.bbadis.2011.09.009
74. A polymorphic position in electron transfer flavoprotein modulates kinetic stability as evidenced by thermal stress
Henriques, B.J., Fisher, M.T., Bross, P., Gomes, C.M.
FEBS Lett (2011) 585, 505-510
https://doi.org/10.1016/j.febslet.2011.01.002
73. Structural reorganization renders enhanced metalloprotein stability
Botelho, H.M., Gomes, C.M.
Chem Commun (Camb) (2011) 47, 11149-11151
https://doi.org/10.1039/c1cc13354c
72. Enhanced superoxide and hydrogen peroxide detection in biological assays
Rodrigues, J.V., Gomes, C.M.
Free radical biology & medicine (2010) 49, 61-66
71. Structural requirements for VAP-B oligomerization and their implication in amyotrophic lateral sclerosis-associated VAP-B(P56S) neurotoxicity
Kim, S., Leal, S.S., Ben Halevy, D., Gomes, C.M., Lev, S.
J Biol Chem (2010) 285, 13839-13849
70. Emerging roles for riboflavin in functional rescue of mitochondrial beta-oxidation flavoenzymes
Henriques, B.J., Olsen, R.K., Bross, P., Gomes, C.M.
Current medicinal chemistry (2010) 17, 3842-3854
69. Mutational hotspots in electron transfer flavoprotein underlie defective folding and function in multiple acyl-CoA dehydrogenase deficiency
Henriques, B.J., Bross, P., Gomes, C.M.
Biochim Biophys Acta (2010) 1802, 1070-1077
68. Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity
Fritz, G., Botelho, H.M., Morozova-Roche, L.A., Gomes, C.M.
The FEBS journal (2010) 277, 4578-4590
67. Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region
Correia, A.R., Wang, T., Craig, E.A., Gomes, C.M.
Biochem J (2010) 426, 197-203
66. Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins
Botelho, H.M., Leal, S.S., Veith, A., Prosinecki, V., Bauer, C., Frohlich, R., Kletzin, A., Gomes, C.M.
J Biol Inorg Chem (2010) 15, 271-281
65. No evidence of direct binding between ursodeoxycholic acid and the p53 DNA-binding domain
Amaral, J.D., Correia, A.R., Steer, C.J., Gomes, C.M., Rodrigues, C.M.
Bioscience reports (2010) 30, 359-364
64. Role of flavinylation in a mild variant of multiple acyl-CoA dehydrogenation deficiency: a molecular rationale for the effects of riboflavin supplementation
Henriques, B.J., Rodrigues, J.V., Olsen, R.K., Bross, P., Gomes, C.M.
J Biol Chem (2009) 284, 4222-4229
63. The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications
Correia, A.R., Ow, S.Y., Wright, P.C., Gomes, C.M.
Biochem Biophys Res Commun (2009) 390, 1007-1011
62. Metal ions modulate the folding and stability of the tumor suppressor protein S100A2
Botelho, H.M., Koch, M., Fritz, G., Gomes, C.M.
The FEBS journal (2009) 276, 1776-1786
61. The prominent conformational plasticity of lactoperoxidase: a chemical and pH stability analysis
Boscolo, B., Leal, S.S., Salgueiro, C.A., Ghibaudi, E.M., Gomes, C.M.
Biochim Biophys Acta (2009) 1794, 1041-1048
60. A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c
Stelter, M., Melo, A.M., Pereira, M.M., Gomes, C.M., Hreggvidsson, G.O., Hjorleifsdottir, S., Saraiva, L.M., Teixeira, M., Archer, M.
Biochemistry (2008) 47, 11953-11963
59. Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning
Leandro, P., Gomes, C.M.
Mini Rev Med Chem (2008) 8, 901-911
58. On the relative contribution of ionic interactions over iron-sulfur clusters to ferredoxin stability
Leal, S.S., Gomes, C.M.
Biochim Biophys Acta (2008) 1784, 1596-1600
57. Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism
Gouveia, R.M., Gomes, C.M., Sousa, M., Alves, P.M., Costa, J.
J Biol Chem (2008) 283, 28038-28047
56. Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+)-containing ferredoxin
Frazao, C., Aragao, D., Coelho, R., Leal, S.S., Gomes, C.M., Teixeira, M., Carrondo, M.A.
FEBS Lett (2008) 582, 763-767
55. On the relation between native geometry and conformational plasticity
Faisca, P.F., Gomes, C.M.
Biophys Chem (2008) 138, 99-106
54. Dynamics, stability and iron-binding activity of frataxin clinical mutants
Correia, A.R., Pastore, C., Adinolfi, S., Pastore, A., Gomes, C.M.
FEBS journal (2008) 275, 3680-3690
53. A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron-Sulfur Moieties
Todorovic, S., Leal, S.S., Salgueiro, C.A., Zebger, I., Hildebrandt, P., Murgida, D.H., Gomes, C.M.
Biochemistry (2007) 46, 10733-10738
52. Conformational states and protein stability in a proteomic perspective.
Prosinecki, V., Faísca, P.F.N., Gomes, C.M.
Current Proteomics (2007) 4, 44-52
51. ApoA-I cleaved by transthyretin has reduced ability to promote cholesterol efflux and increased amyloidogenicity
Liz, M.A., Gomes, C.M., Saraiva, M.J., Sousa, M.M.
J Lipid Res (2007) 48, 2385-2395
50. Studies of the molten globule state of ferredoxin: Structural characterization and implications on protein folding and iron-sulfur center assembly
Leal, S.S., Gomes, C.M.
Proteins (2007) 68, 606-616
49. Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: A thermal unfolding study
Boscolo, B., Leal, S.S., Ghibaudi, E.M., Gomes, C.M.
Biochim Biophys Acta (2007) 1774, 1164-1172
48. X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme
Urich, T., Gomes, C.M., Kletzin, A., Frazao, C.
Science (2006) 311, 996-1000
47. Natural domain design: enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site
Rocha, R., Leal, S.S., Teixeira, V.H., Regalla, M., Huber, H., Baptista, A.M., Soares, C.M., Gomes, C.M.
Biochemistry (2006) 45, 10376-10384
46. A Proteomic Approach toward the Selection of Proteins with Enhanced Intrinsic Conformational Stability
Prosinecki, V., Botelho, H.M., Francese, S., Mastrobuoni, G., Moneti, G., Urich, T., Kletzin, A., Gomes, C.M.
J Proteome Res (2006) 5, 2720-2726
45. Combined spectroscopic and calorimetric characterisation of rubredoxin reversible thermal transition
Henriques, B.J., Saraiva, L.M., Gomes, C.M.
J Biol Inorg Chem (2006) 11, 73-81
44. Conformational stability of human frataxin and effect of Friedreich's ataxia-related mutations on protein folding
Correia, A.R., Adinolfi, S., Pastore, A., Gomes, C.M.
Biochem J (2006) 398, 605-611
43. Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins
Leal, S.S., Gomes, C.M.
Biol Chem (2005) 386, 1295-1300
42. A Rieske ferredoxin typifying a subtype within Rieske proteins: spectroscopic, biochemical and stability studies
Kletzin, A., Ferreira, A.S., Hechler, T., Bandeiras, T.M., Teixeira, M., Gomes, C.M.
FEBS Lett (2005) 579, 1020-1026
41. Probing the mechanism of rubredoxin thermal unfolding in the absence of salt bridges by temperature jump experiments
Henriques, B.J., Saraiva, L.M., Gomes, C.M.
Biochem Biophys Res Commun (2005) 333, 839-844
40. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre
Urich, T., Bandeiras, T.M., Leal, S.S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C.M., Kletzin, A.
Biochem J (2004) 381, 137-146
39. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase
Muller, F.H., Bandeiras, T.M., Urich, T., Teixeira, M., Gomes, C.M., Kletzin, A.
Mol Microbiol (2004) 53, 1147-1160
38. Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: cluster dissociation, iron release and protein stability
Leal, S.S., Teixeira, M., Gomes, C.M.
J Biol Inorg Chem (2004) 9, 987-996
37. Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea
Kletzin, A., Urich, T., Muller, F., Bandeiras, T.M., Gomes, C.M.
J Bioenerg Biomembr (2004) 36, 77-91
36. Active site structure of the aa3 quinol oxidase of Acidianus ambivalens
Das, T.K., Gomes, C.M., Bandeiras, T.M., Pereira, M.M., Teixeira, M., Rousseau, D.L.
Biochim Biophys Acta (2004) 1655, 306-320
35. Docking and electron transfer studies between rubredoxin and rubredoxin:oxygen oxidoreductase
Victor, B.L., Vicente, J.B., Rodrigues, R., Oliveira, S., Rodrigues-Pousada, C., Frazao, C., Gomes, C.M., Teixeira, M., Soares, C.M.
J Biol Inorg Chem (2003) 8, 475-488
34. FTIR spectroscopic characterization of the cytochrome aa3 from Acidianus ambivalens: evidence for the involvement of acidic residues in redox coupled proton translocation
Hellwig, P., Gomes, C.M., Teixeira, M.
Biochemistry (2003) 42, 6179-6184
33. The respiratory chain of the thermophilic archaeon Sulfolobus metallicus: studies on the type-II NADH dehydrogenase
Bandeiras, T.M., Salgueiro, C.A., Huber, H., Gomes, C.M., Teixeira, M.
Biochim Biophys Acta (2003) 1557, 13-19
32. Module fusion in an A-type flavoprotein from the cyanobacterium Synechocystis condenses a multiple-component pathway in a single polypeptide chain
Vicente, J.B., Gomes, C.M., Wasserfallen, A., Teixeira, M.
Biochem Biophys Res Commun (2002) 294, 82-87
31. Plasticity of proton pathways in haem-copper oxygen reductases
Pereira, M.M., Gomes, C.M., Teixeira, M.
FEBS Lett (2002) 522, 14-18
30. The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: spectroscopic and redox studies
Lemos, R.S., Gomes, C.M., LeGall, J., Xavier, A.V., Teixeira, M.
J Bioenerg Biomembr (2002) 34, 21-30
29. Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment
Lemos, R.S., Fernandes, A.S., Pereira, M.M., Gomes, C.M., Teixeira, M.
Biochim Biophys Acta (2002) 1553, 158-170
28. Formation of a linear [3Fe-4S] cluster in a seven-iron ferredoxin triggered by polypeptide unfolding
Jones, K., Gomes, C.M., Huber, H., Teixeira, M., Wittung-Stafshede, P.
J Biol Inorg Chem (2002) 7, 357-362
27. An archaeal b-type cytochrome containing a nonfunctional carbonic anhydrase-like domain
Gomes, C.M., Kletzin, A., Teixeira, M.
J Biol Inorg Chem (2002) 7, 483-489
26. A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin
Gomes, C.M., Giuffre, A., Forte, E., Vicente, J.B., Saraiva, L.M., Brunori, M., Teixeira, M.
J Biol Chem (2002) 277, 25273-25276
https://doi.org/doi: 10.1074/jbc.M203886200
25. Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements
Gomes, C.M., Frazao, C., Xavier, A.V., Legall, J., Teixeira, M.
Protein Sci (2002) 11, 707-712
24. Acidianus ambivalens type-II NADH dehydrogenase: genetic characterisation and identification of the flavin moiety as FMN
Bandeiras, T.M., Salgueiro, C., Kletzin, A., Gomes, C.M., Teixeira, M.
FEBS Lett (2002) 531, 273-277
23. High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactors
Moczygemba, C., Guidry, J., Jones, K.L., Gomes, C.M., Teixeira, M., Wittung-Stafshede, P.
Protein Sci (2001) 10, 1539-1548
22. Acidianus ambivalens Complex II typifies a novel family of succinate dehydrogenases
Lemos, R.S., Gomes, C.M., Teixeira, M.
Biochem Biophys Res Commun (2001) 281, 141-150
21. The 'strict' anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain
Lemos, R.S., Gomes, C.M., Santana, M., LeGall, J., Xavier, A.V., Teixeira, M.
FEBS Lett (2001) 496, 40-43
20. Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
Gomes, C.M., Le Gall, J., Xavier, A.V., Teixeira, M.
Chembiochem (2001) 2, 583-587
19. A new type-II NADH dehydrogenase from the archaeon Acidianus ambivalens: characterization and in vitro reconstitution of the respiratory chain
Gomes, C.M., Bandeiras, T.M., Teixeira, M.
J Bioenerg Biomembr (2001) 33, 1-8
18. Heme-copper oxidases with modified D- and K-pathways are yet efficient proton pumps
Gomes, C.M., Backgren, C., Teixeira, M., Puustinen, A., Verkhovskaya, M.L., Wikstrom, M., Verkhovsky, M.I.
FEBS Lett (2001) 497, 159-164
17. Kinetics of electron and proton transfer during O(2) reduction in cytochrome aa(3) from A. ambivalens: an enzyme lacking Glu(I-286)
Gilderson, G., Aagaard, A., Gomes, C.M., Adelroth, P., Teixeira, M., Brzezinski, P.
Biochim Biophys Acta (2001) 1503, 261-270
16. Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens
Wittung-Stafshede, P., Gomes, C.M., Teixeira, M.
J Inorg Biochem (2000) 78, 35-41
15. Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner
Gomes, C.M., Vicente, J.B., Wasserfallen, A., Teixeira, M.
Biochemistry (2000) 39, 16230-16237
14. Structure of a dioxygen reduction enzyme from Desulfovibrio gigas
Frazao, C., Silva, G., Gomes, C.M., Matias, P., Coelho, R., Sieker, L., Macedo, S., Liu, M.Y., Oliveira, S., Teixeira, M., Xavier, A.V., Rodrigues-Pousada, C., Carrondo, M.A., Le Gall, J.
Nat Struct Biol (2000) 7, 1041-1045
13. Desulfovibrio gigas neelaredoxin. A novel superoxide dismutase integrated in a putative oxygen sensory operon of an anaerobe
Silva, G., Oliveira, S., Gomes, C.M., Pacheco, I., Liu, M.Y., Xavier, A.V., Teixeira, M., Legall, J., Rodrigues-pousada, C.
Eur J Biochem (1999) 259, 235-243
12. The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774
Romao, C.V., Liu, M.Y., Le Gall, J., Gomes, C.M., Braga, V., Pacheco, I., Xavier, A.V., Teixeira, M.
Eur J Biochem (1999) 261, 438-443
11. The unusual iron sulfur composition of the Acidianus ambivalens succinate dehydrogenase complex
Gomes, C.M., Lemos, R.S., Teixeira, M., Kletzin, A., Huber, H., Stetter, K.O., Schafer, G., Anemuller, S.
Biochim Biophys Acta (1999) 1411, 134-141
10. Redox-linked transient deprotonation at the binuclear site in the aa(3)-type quinol oxidase from Acidianus ambivalens: implications for proton translocation
Das, T.K., Gomes, C.M., Teixeira, M., Rousseau, D.L.
Proc Natl Acad Sci U S A (1999) 96, 9591-9596
9. Dynamics of the binuclear center of the quinol oxidase from Acidianus ambivalens
Aagaard, A., Gilderson, G., Gomes, C.M., Teixeira, M., Brzezinski, P.
Biochemistry (1999) 38, 10032-10041
8. Characterisation of a new rubredoxin isolated from Desulfovibrio desulfuricans 27774: definition of a new family of rubredoxins
LeGall, J., Liu, M.Y., Gomes, C.M., Braga, V., Pacheco, I., Regalla, M., Xavier, A.V., Teixeira, M.
FEBS Lett (1998) 429, 295-298
7. Ambineela, an unusual blue protein isolated from the archaeon Acidianus ambivalens
Gomes, C.M., Teixeira, M.
Biochem Biophys Res Commun (1998) 249, 23-25
6. The NADH oxidase from the thermoacidophilic archaea Acidianus ambivalens: isolation and physicochemical characterisation
Gomes, C.M., Teixeira, M.
Biochem Biophys Res Commun (1998) 243, 412-415
5. Evidence for a novel type of iron cluster in the respiratory chain of the archaeon Sulfolobus metallicus
Gomes, C.M., Huber, H., Stetter, K.O., Teixeira, M.
FEBS Lett (1998) 432, 99-102
4. Di-cluster, seven-iron ferredoxins from hyperthermophilic Sulfolobales
Gomes, C.M., Faria, A., Carita, J.C., Mendes, J., Regalla, M., Chicau, P., Huber, H., Stetter, K.O., Teixeira, M.
J Biol Inorg Chem (1998) 3, 499-507
3. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
Gomes, C.M., Silva, G., Oliveira, S., LeGall, J., Liu, M.Y., Xavier, A.V., Rodrigues-Pousada, C., Teixeira, M.
J Biol Chem (1997) 272, 22502-22508
2. Functional properties of the quinol oxidase from Acidianus ambivalens and the possible catalytic role of its electron donor-studies on the membrane-integrated and purified enzyme
Giuffre, A., Gomes, C.M., Antonini, G., D'Itri, E., Teixeira, M., Brunori, M.
Eur J Biochem (1997) 250, 383-388
1. A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens
Teixeira, M., Batista, R., Campos, A.P., Gomes, C., Mendes, J., Pacheco, I., Anemuller, S., Hagen, W.R.
Eur J Biochem (1995) 227, 322-327