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An NMR structural study of nickel-substituted rubredoxin
Goodfellow, Brian J.; Duarte, Iven C. N.; Macedo, Anjos L.; Volkman, Brian F.; Nunes, Sofia G.; Moura, Isabel; Markley, John L.; Moura, José J. G.J Biol Inorg Chem (2010) 15:409–420 DOI 10.1007/s00775-009-0613-6 ; The Ni(II) and Zn(II) derivatives of Desulfovibrio vulgaris rubredoxin (DvRd) have been studied by NMR spectroscopy to probe the structure at the metal centre. The βCH2 proton pairs from the cysteines that bind the Ni(II) atom have been identified using 1D nuclear Overhauser enhancement (NOE) difference spectra and sequence specifically assign...
Crystal Structure of the VV Dimer [V2O2(μ-O)(dmpp)2(OCH3)2] and Its Equilibrium...
Avecilla, Fernando; Geraldes, Carlos F. G. C.; Macedo, Anjos L.; Castro, M. Margarida C. A.The behaviour of the cyclic trimeric VV complex [V3O3(μ-O)3(dmpp)3(H2O)](H2O)2, V3L3, (L = Hdmpp = 3-hydroxy-1,2-dimethyl-4-pyridinone) was studied in methanol and methanol/water solutions by using 51V and 1D- and 2D 1H NMR spectroscopy. Red crystals, isolated from a highly concentrated methanol solution of the trimeric complex, were analysed by X-ray crystallography. The solid-state structure of the compound s...
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] ...
Rodrigues, Pedro M.; Macedo, Anjos L.; Moura, Isabel; Moura, José J. G.; Goodfellow, Brian J.J Biol Inorg Chem (2006) 11: 307–315 DOI 10.1007/s00775-005-0077-2 ; Desulfovibrio gigas ferredoxin II (DgFdII) is a small protein with a polypeptide chain composed of 58 amino acids, containing one Fe3S4 cluster per monomer. Upon studying the redox cycle of this protein, we detected a stable intermediate (FdIIint) with four 1H resonances at 24.1, 20.5, 20.8 and 13.7 ppm. The differences between FdIIox and FdI...
Spectroscopic characterization of a novel 2 /[4Fe /4S] ferredoxin isolated from...
Moura, José J. G.; Rodrigues, Pedro M.; Moura, Isabel; Macedo, Anjos L.Inorganica Chimica Acta 356 (2003) 215-221 ; A novel iron /sulfur containing protein, a ferredoxin (Fd), was purified to homogeneity from the extract of Desulfovibrio desulfuricans American type culture collection (ATCC) 27774. The purified protein is a 13.4 kDa homodimer with a polypeptide chain of 60 amino acids residues, containing eight cysteines that coordinate two [4Fe /4S] clusters. The protein is shown...
Copper complexes with bibracchial lariat ethers: from mono- to binuclear struct...
Rodríguez-Infante, Covadonga; Esteban, David; Avecilla, Fernando; Blas, Andrés de; Rodríguez-Blas, Teresa; Mahía, Jose; Macedo, Anjos L.Copper(II) complexes with a series of bibracchial lariat ethers are described. Independently of the nature of the counterion present (nitrate or perchlorate), the lariat ether N,N'-bis(2-aminobenzyl)-1,10-diaza-15-crown-5 (L1) always forms mononuclear complexes, whereas the lariat ethers N,N'-bis(2-aminobenzyl)-4,13-diaza-18-crown-6 (L2) and N,N'-bis(2-salicylaldiminobenzyl)-4,13-diaza-18-crown-6 (L3) only give...
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