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New spectroscopic and electrochemical insights on a class I superoxide reductas...

Folgosa, Filipe; Cordas, Cristina M.; Santos, Joana A.; Pereira, Alice S.; Moura, José J. G.; Tavares, Pedro; Moura, Isabel

Biochem. J. (2011) 438,485–494 doi:10.1042/BJ20110836

Data: 2011   |   Origem: Repositório Institucional da UNL

Low-Spin Heme b3 in the Catalytic Center of Nitric Oxide Reductase from Pseudom...

Timóteo, Cristina G.; Pereira, Alice S.; Martins, Carlos E.; Naik, Sunil G.; Duarte, Américo G.; Moura, José J. G.; Tavares, Pedro; Moura, Isabel

Biochemistry, 2011, 50 (20), pp 4251–4262 DOI: 10.1021/bi101605p ; Respiratory nitric oxide reductase (NOR) was purified from membrane extract of Pseudomonas (Ps.) nautica cells to homogeneity as judged by polyacrylamide gel electrophoresis. The purified protein is a heterodimer with subunits of molecular masses of 54 and 18 kDa. The gene encoding both subunits was cloned and sequenced. The amino acid sequence...

Data: 2011   |   Origem: Repositório Institucional da UNL

Camelid nanobodies raised against an integral membrane enzyme, nitric oxide red...

Conrath, Katja; Pereira, Alice S.; Martins, Carlos E.; Timóteo, Cristina G.; Tavares, Pedro; Moura, Isabel; Moura, José J. G.

Protein Sci. 2009 Mar;18(3):619-28. doi: 10.1002/pro.69. ; Nitric Oxide Reductase (NOR) is an integral membrane protein performing the reduction of NO to N2O. NOR is composed of two subunits: the large one (NorB) is a bundle of 12 transmembrane helices (TMH). It contains a b type heme and a binuclear iron site, which is believed to be the catalytic site, comprising a heme b and a non-hemic iron. The small subu...

Data: 2009   |   Origem: Repositório Institucional da UNL

Molybdenum Induces the expression of a protein containing a new heterometallic ...

Rivas, Maria G.; Carepo, Marta S. P.; Mota, Cristiano S.; Moura, José J. G.; Moura, Isabel; Korbas, Malgorzata; Lopes, Ana T.; Brondino, Carlos D.

Biochemistry. 2009 Feb 10;48(5):873-82. doi: 10.1021/bi801773t. ; The characterization of a novel Mo-Fe protein (MorP) associated with a system that responds to Mo in Desulfovibrio alaskensis is reported. Biochemical characterization shows that MorP is a periplasmic homomultimer of high molecular weight (260 +/- 13 kDa) consisting of 16-18 monomers of 15321.1 +/- 0.5 Da. The UV/visible absorption spectrum of t...

Data: 2009   |   Origem: Repositório Institucional da UNL

Electron transfer complex between nitrous oxide reductase and cytochrome c552 f...

Moura, Isabel; Moura, José J. G.; Pauleta, Sofia R; Monzani, Enrico; Pereira, Alice S.; Casella, Luigi; Dell’Acqua, Simone

Biochemistry. 2008 Oct 14;47(41):10852-62. doi: 10.1021/bi801375q ; The multicopper enzyme nitrous oxide reductase (N 2OR) catalyzes the final step of denitrification, the two-electron reduction of N 2O to N 2. This enzyme is a functional homodimer containing two different multicopper sites: CuA and CuZ. CuA is a binuclear copper site that transfers electrons to the tetranuclear copper sulfide CuZ, the catalyt...

Data: 2008   |   Origem: Repositório Institucional da UNL

NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a no...

Pauleta, Sofia R.; Duarte, Américo G; Carepo, Marta S.; Pereira, Alice S.; Tavares, Pedro; Moura, Isabel; Moura, José J. G.

Biomol NMR Assign (2007) 1:81–83 DOI 10.1007/s12104-007-9022-3 ; We report the 98% assignment of the apo-form of an orange protein, containing a novel Mo–Cu cluster isolated from Desulfovibrio gigas. This protein presents a region where backbone amide protons exchange fast with bulk solvent becoming undetectable. These residues were assigned using 13C-detection experiments.

Data: 2007   |   Origem: Repositório Institucional da UNL

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