Search Results - "Bursakov, S. A"

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    Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas by Bursakov, S A, Gavel, O Yu, Di Rocco, G, Lampreia, J, Calvete, J, Pereira, A S, Moura, J J G, Moura, I

    Published in Journal of inorganic biochemistry (01-05-2004)
    “…An orange-coloured protein (ORP) isolated from Desulfovibrio gigas, a sulphate reducer, has been previously shown by extended X-ray absorption fine structure…”
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    Enzymatic properties and effect of ionic strength on periplasmic nitrate reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774 by Bursakov, S A, Carneiro, C, Almendra, M J, Duarte, R O, Caldeira, J, Moura, I, Moura, J J

    “…Some sulfate reducing bacteria can induce nitrate reductase when grown on nitrate containing media being involved in dissimilatory reduction of nitrate, an…”
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    Microbial and plant metabolism of NO by Payne, W. J., Liu, M.-Y., Bursakov, S. A., Le Gall, J.

    Published in BioFactors (Oxford) (1997)
    “…During microbial denitrification, NO is produced by reduction of nitrite by either the reduced high spin d1 hemes in a unique reductase (NIR) or at the expense…”
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    ATP Sulfurylases from Sulfate-Reducing Bacteria of the Genus Desulfovibrio. A Novel Metalloprotein Containing Cobalt and Zinc by Gavel, Olga Yu, Bursakov, Sergey A, Calvete, Juan J, George, Graham N, Moura, José J. G, Moura, Isabel

    Published in Biochemistry (Easton) (17-11-1998)
    “…Adenosine triphosphate sulfurylase catalyzes the formation of adenosine 5‘-phosphosulfate from adenosine triphosphate and sulfate. The enzyme plays a crucial…”
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    Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas by Gavel, Olga Yu, Bursakov, Sergey A, Pina, David G, Zhadan, Galina G, Moura, José J.G, Moura, Isabel, Shnyrov, Valery L

    Published in Biophysical chemistry (01-07-2004)
    “…A novel adenylate kinase (AK) has recently been purified from Desulfovibrio gigas and characterized as a Co 2+/Zn 2+-containing enzyme: this is an unusual…”
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    Journal Article