Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Amanda K. Chaplin, Jonathan A. R. Worrall, Erik Vijgenboom, Vassiliy N. Bavro, Michael T. Wilson, Jordi Paps, Michael A. Hough, Megan L. Straw
Publikováno v:
Metallomics, 10(1), 180-193. OXFORD UNIV PRESS
Metallomics
Metallomics
Streptomyces lividans has a distinct dependence on the bioavailability of copper for its morphological development. A cytosolic copper resistance system is operative in S. lividans that serves to preclude deleterious copper levels. This system compri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::681a7d249fbab6f8edf28b9258389ed7
http://hdl.handle.net/1887/3217486
http://hdl.handle.net/1887/3217486
Publikováno v:
Biophysical Chemistry. 98:65-77
The iron ligand, Met80, of yeast iso-1-cytochrome c has been mutated to residues that are unable to bind to the iron. The resultant proteins, Met80Ala, Ser, Asp, Glu, have been expressed and purified. All mutant proteins exhibit well defined pH depen
Autor:
Magda Gioia, Brandon J. Reeder, Alessandra Pesce, Fabio Polticelli, Michael T. Wilson, Massimo Coletta, Paolo Ascenzi, Marco Nardini, Maria Marino, Martino Bolognesi, Stefano Marini
Publikováno v:
Biochimica et biophysica acta. 1834(9)
Multimeric globins (e.g., hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric globins (e.g., myoglobin; Mb) usually are assumed to be non-allosteric. However, the modulation of the functional properties of monomer
Autor:
Michael J. Osborne, Graham S. Bailey, Geoffrey R. Moore, Michael T. Wilson, Talal S. El-Thaher
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1160:235-238
The 1H-NMR spectra have been obtained for rat submandibular kallikrein in the absence and presence of inhibitors. Two competitive inhibitors were investigated, the tripeptide leupeptin (a potent inhibitor with Ki 0.5 microM) and a hexapeptide (a much
Publikováno v:
Biochimica et biophysica acta. 1655(1-3)
It has been reported that different amino acid radicals are formed following the addition of hydrogen peroxide to cytochrome c oxidase (CcO) from bovine heart or from Paracoccus denitrificans. A broad unresolved signal in the electron paramagnetic re
Publikováno v:
Biochemistry. 35(33)
Utilizing a recently developed novel fluorescence technique [Wall et al. (1995) Mol. Membr. Biol. 12, 183-192], it is shown that the interactions of p25, the leader peptide of subunit IV of cytochrome c oxidase, with phospholipid membranes can be ide
Autor:
Michael J. Fryer, Michael T. Wilson, Brandon J. Reeder, Dimitri A. Svistunenko, Peter Nicholls, Jacqueline Dunne, Chris E. Cooper, Francesca Cutruzzolà, Maria Giulia Bigotti
Publikováno v:
Biophysical Journal. (5):2845-2855
The reactions of hydrogen peroxide with human methemoglobin, sperm whale metmyoglobin, and horse heart metmyoglobin were studied by electron paramagnetic resonance (EPR) spectroscopy at 10 K and room temperature. The singlet EPR signal, one of the th
Publikováno v:
FEBS letters. 257(1)
Dimeric and monomeric forms of mitochondrial cytochrome oxidase (EC 1.9.3.1) have been examined using 1H NMR spectroscopy. Paramagnetically shifted resonances were detected in spectra of the monomeric protein. Studies of this protein in a number of o