Zobrazeno 31 - 40
of 40
pro vyhledávání: '"Michael T. Wilson"'
Publikováno v:
FEBS Letters. (4):507-512
Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the diss
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
Autor:
John R. Guest, Simon C. Andrews, Michael T. Wilson, Pauline M. Harrison, Andrew J. Thomson, Nick E. Le Brun, Geoffrey R. Moore
Publikováno v:
FEBS Letters. (1-2):197-202
The mechanism by which iron-storage proteins take up and oxidise iron(II) is not understood. We show by rapid-kinetic and EPR measurements that iron uptake, in vitro, by a bacterial iron-storage protein, bacterioferritin, involves at least three kine
Publikováno v:
FEBS Letters. (1-3):29-32
We have used optical and electron paramagnetic spectroscopy to study the flavohaem enzyme cellobiose oxidoreductase (CBOR) from Phanerochaete chrysosporium. We have examined redox cycles of the enzyme in which the oxidation of cellobiose to cellobion
Publikováno v:
Cytochrome Systems ISBN: 9781461290780
The name “pulsed” oxidase was initially assigned to the transient species observed upon exposure of reduced cytochrome c oxidase, in the presence of cytochrome c and excess ascorbate, to a pulse of dioxygen (1). The pulsed species obtained accord
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e4b44a1ec6b6ef6153dc7c92cbbb875
https://doi.org/10.1007/978-1-4613-1941-2_97
https://doi.org/10.1007/978-1-4613-1941-2_97
Publikováno v:
Biochemical and biophysical research communications. 99(1)
The polypeptide subunits of cytochrome c oxidase (E.C. 1.9.3.1.) isolated from beef heart which react with 203 [Hg]Cl 2 have been identified. A rapid and simple method for identifying and numbering the subunits is described which is independent of 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
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. :S57-S58
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. :e101
Publikováno v:
Structure and Dynamics of Nucleic Acids, Proteins, and Membranes ISBN: 9781468453102
Cytochrome-c-oxidase, an integral membrane protein of the inner mitrochondrial membrane, is the terminal enzyme of the respiratory chain. This paper summarizes the role of this enzyme in energy conservation, and presents a possible regulatory model b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::766164232bd0128b666cf9a42f8c92b2
https://hdl.handle.net/11590/159840
https://hdl.handle.net/11590/159840
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