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Multinuclear blue copper-proteins: the evolutionary design. / Moshkov, K.A.; Zaitsev, V.N.; Grishina, T.V.; Stefanov, V.E.

в: Journal of Evolutionary Biochemistry and Physiology, Том 50, № 3, 2014, стр. 189-205.

Результаты исследований: Научные публикации в периодических изданияхОбзор литературы

Harvard

Moshkov, KA, Zaitsev, VN, Grishina, TV & Stefanov, VE 2014, 'Multinuclear blue copper-proteins: the evolutionary design', Journal of Evolutionary Biochemistry and Physiology, Том. 50, № 3, стр. 189-205. https://doi.org/10.1134/S0022093014030016

APA

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Author

Moshkov, K.A. ; Zaitsev, V.N. ; Grishina, T.V. ; Stefanov, V.E. / Multinuclear blue copper-proteins: the evolutionary design. в: Journal of Evolutionary Biochemistry and Physiology. 2014 ; Том 50, № 3. стр. 189-205.

BibTeX

@article{03d613167d664919b33a48f3f437c5d7,
title = "Multinuclear blue copper-proteins: the evolutionary design",
abstract = "The review presents both our own and literature data on studies of pathways of evolution of the so-called multinuclear blue copper-proteins (MBCP) that have the domain organization. The MBCP are widely spread in living nature, they have been revealed in cells of archei, bacteria, and eukaryotes. The MBCP composition includes the copper-proteins such different by their properties as oxidases, reductase, blood coagulation factors V and VIII. Most likely, MBCP have been originated from a low-molecular protein-precursor similar topologically with the blue electron-transporting protein of the cupredoxin type, as a result of action of various evolutionary mechanisms: amplification of genes, formation of protein structures by different combinations of domains, a change of size of domains, the segment elongation at the expense of the activational domain, formation and loss of copper-binding centers, variation of amino acid ligands in such centers, the appearance of centers of binding of other proteins, glycosylation,",
author = "K.A. Moshkov and V.N. Zaitsev and T.V. Grishina and V.E. Stefanov",
year = "2014",
doi = "10.1134/S0022093014030016",
language = "English",
volume = "50",
pages = "189--205",
journal = "Journal of Evolutionary Biochemistry and Physiology",
issn = "0022-0930",
publisher = "Pleiades Publishing",
number = "3",

}

RIS

TY - JOUR

T1 - Multinuclear blue copper-proteins: the evolutionary design

AU - Moshkov, K.A.

AU - Zaitsev, V.N.

AU - Grishina, T.V.

AU - Stefanov, V.E.

PY - 2014

Y1 - 2014

N2 - The review presents both our own and literature data on studies of pathways of evolution of the so-called multinuclear blue copper-proteins (MBCP) that have the domain organization. The MBCP are widely spread in living nature, they have been revealed in cells of archei, bacteria, and eukaryotes. The MBCP composition includes the copper-proteins such different by their properties as oxidases, reductase, blood coagulation factors V and VIII. Most likely, MBCP have been originated from a low-molecular protein-precursor similar topologically with the blue electron-transporting protein of the cupredoxin type, as a result of action of various evolutionary mechanisms: amplification of genes, formation of protein structures by different combinations of domains, a change of size of domains, the segment elongation at the expense of the activational domain, formation and loss of copper-binding centers, variation of amino acid ligands in such centers, the appearance of centers of binding of other proteins, glycosylation,

AB - The review presents both our own and literature data on studies of pathways of evolution of the so-called multinuclear blue copper-proteins (MBCP) that have the domain organization. The MBCP are widely spread in living nature, they have been revealed in cells of archei, bacteria, and eukaryotes. The MBCP composition includes the copper-proteins such different by their properties as oxidases, reductase, blood coagulation factors V and VIII. Most likely, MBCP have been originated from a low-molecular protein-precursor similar topologically with the blue electron-transporting protein of the cupredoxin type, as a result of action of various evolutionary mechanisms: amplification of genes, formation of protein structures by different combinations of domains, a change of size of domains, the segment elongation at the expense of the activational domain, formation and loss of copper-binding centers, variation of amino acid ligands in such centers, the appearance of centers of binding of other proteins, glycosylation,

U2 - 10.1134/S0022093014030016

DO - 10.1134/S0022093014030016

M3 - Literature review

VL - 50

SP - 189

EP - 205

JO - Journal of Evolutionary Biochemistry and Physiology

JF - Journal of Evolutionary Biochemistry and Physiology

SN - 0022-0930

IS - 3

ER -

ID: 7034762