Proton migration in a stack of tyrosine molecules by the action of Mg2+ and electric field. A mathematical model

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Proton migration in a stack of tyrosine molecules by the action of Mg²⁺ and electric field. A mathematical model. / Tulub, A. A.; Stefanov, V. E.; Skaletskii, E. K.

в: Biofizika, Том 46, № 4, 2001, стр. 587-588.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

BibTeX

@article{23352ce4d33e46289bf573dc39229d49,

title = "Proton migration in a stack of tyrosine molecules by the action of Mg2+ and electric field. A mathematical model",

abstract = "Quantum chemistry methods (ab initio, RHF + MP2(FULL), 6-31G** basis set) were used to study proton migration in tyrosine stacks mimicking the proton channel in tubulin and other proteins. When bound to guanosine-5′-triphosphate, Mg2+ favors the dissociation of water in its first coordination shell, thus initiating subsequent proton shifts in the tyrosine chain composed of spatially remote tyrosine residues of tubulin. The process appears to be thermodynamically allowed, ΔG298 < 0 with a potential barrier along the proton shift of no more than 0.75 kcal/mol. The exposure to external electrical field of low intensity, which simulates the elektret properties of tubulin, promotes proton migration over long distances.",

keywords = "External electrical field, Hydrogen bond, Magnesium cofactor, Proton migration, Quantum chemistry, Tubulin",

author = "Tulub, {A. A.} and Stefanov, {V. E.} and Skaletskii, {E. K.}",

year = "2001",

language = "English",

volume = "46",

pages = "587--588",

journal = "БИОФИЗИКА",

issn = "0006-3029",

publisher = "Издательство {"}Наука{"}",

number = "4",

}

RIS

TY - JOUR

T1 - Proton migration in a stack of tyrosine molecules by the action of Mg2+ and electric field. A mathematical model

AU - Tulub, A. A.

AU - Stefanov, V. E.

AU - Skaletskii, E. K.

PY - 2001

Y1 - 2001

N2 - Quantum chemistry methods (ab initio, RHF + MP2(FULL), 6-31G** basis set) were used to study proton migration in tyrosine stacks mimicking the proton channel in tubulin and other proteins. When bound to guanosine-5′-triphosphate, Mg2+ favors the dissociation of water in its first coordination shell, thus initiating subsequent proton shifts in the tyrosine chain composed of spatially remote tyrosine residues of tubulin. The process appears to be thermodynamically allowed, ΔG298 < 0 with a potential barrier along the proton shift of no more than 0.75 kcal/mol. The exposure to external electrical field of low intensity, which simulates the elektret properties of tubulin, promotes proton migration over long distances.

AB - Quantum chemistry methods (ab initio, RHF + MP2(FULL), 6-31G** basis set) were used to study proton migration in tyrosine stacks mimicking the proton channel in tubulin and other proteins. When bound to guanosine-5′-triphosphate, Mg2+ favors the dissociation of water in its first coordination shell, thus initiating subsequent proton shifts in the tyrosine chain composed of spatially remote tyrosine residues of tubulin. The process appears to be thermodynamically allowed, ΔG298 < 0 with a potential barrier along the proton shift of no more than 0.75 kcal/mol. The exposure to external electrical field of low intensity, which simulates the elektret properties of tubulin, promotes proton migration over long distances.

KW - External electrical field

KW - Hydrogen bond

KW - Magnesium cofactor

KW - Proton migration

KW - Quantum chemistry

KW - Tubulin

UR - http://www.scopus.com/inward/record.url?scp=0042870264&partnerID=8YFLogxK

M3 - Article

C2 - 11558365

AN - SCOPUS:0042870264

VL - 46

SP - 587

EP - 588

JO - БИОФИЗИКА

JF - БИОФИЗИКА

SN - 0006-3029

IS - 4

ER -

ID: 89840623