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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/1535

Título: Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
Autor: Moura, José J. G.
Moura, Isabel
Gavel, Olga Yu.
Bursakov, Sergey A.
Pina, David G.
Zhadan, Galina G.
Shnyrov, Valery L.
Palavras-chave: Protein stability
Differential scanning calorimetry
Circular dichroism
Intrinsic fluorescence
Adenylate kinase
Desulfovibrio gigas
Issue Date: Apr-2004
Editora: Elsevier
Resumo: A novel adenylate kinase (AK) has recently been purified from Desulfovibrio gigas and characterized as a Co2+/Zn2+-containing enzyme: this is an unusual characteristic for AKs from Gram-negative bacteria, in which these enzymes are normally devoid of metals. Here, we studied the conformational stability of holo- and apo-AK as a function of temperature by differential scanning calorimetry (DSC), circular dichroism (CD), and intrinsic fluorescence spectroscopy. The thermal unfolding of AK is a cooperative two-state process, and is sufficiently reversible in the 9–11 pH range, that can be correctly interpreted in terms of a simple two-state thermodynamic model. The spectral parameters as monitored by ellipticity changes in the CD spectra of the enzyme as well as the decrease in tryptophan intensity emission upon heating were seen to be good complements to the highly sensitive but integral DSC-method.
Descrição: Biophysical Chemistry 110 (2004) 83–92
URI: http://hdl.handle.net/10362/1535
ISSN: 0301-4622
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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