Výsledky vyhledávání - "I A, Tukhvatullin"

Revealing of the cation-binding sites on the surface of hemoglobin in its reaction with the NO donor, the nitrosyl iron complex {Fe2[S(CH2)2NH3]2(NO)4}SO4·2.5H2O

Autor: T. N. Rudneva, L. A. Syrtsova, I. A. Tukhvatullin, N. I. Shkondina, Natalia A. Sanina, Alexander I. Kotelnikov, S. M. Aldoshin, B. L. Psikha

Publikováno v: Russian Chemical Bulletin. 61:2350-2355

Deoxyhemoglobin (Hb) stabilizes the cationic nitrosyl iron complex with cysteamine {Fe2[S(CH2)2NH3]2(NO)4}SO4·2.5H2O (CysAm), by slowing down its hydrolysis. In the absence of Hb, the electrochemical detection of NO release in the course of the hydr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a014b31de7175b99bba48f4d8873e362
https://doi.org/10.1007/s11172-012-0330-0

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Purification and properties of membrane-bound methane hydroxylase from Methylococcus capsulatus (Strain M)

Autor: R. I. Gvozdev, L. V. Tumanova, I. A. Tukhvatullin

Publikováno v: Biology Bulletin. 35:161-169

Membrane fraction of Methylococcus capsulatus (strain M) were treated with [14C]acetylene, an affinity label binding to the active center of membrane-bound methane monooxygenase (MMO). High-purity particulate form of methane hydroxylase (pMH) was obt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8c4fc58c103c1506e8f6fab7fee61e1f
https://doi.org/10.1134/s1062359008020106

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Optimization of solubilization and purification procedures for the hydroxylase component of membrane-bound methane monooxygenase from Methylococcus capsulatus strain M

Autor: R. I. Gvozdev, I. A. Tukhvatullin, Tamara V. Tikhonova, V. I. Vasil’ev, Vladimir Popov

Publikováno v: Biochemistry (Moscow). 71:1329-1335

The hydroxylase component of membrane-bound (particulate) methane monooxygenase (pMMO) from Methylococcus capsulatus strain M was isolated and purified to homogeneity. The pMMO molecule comprises three subunits of molecular masses 47, 26, and 23 kD a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::591230cb5024119976b1d9e075f57cd3
https://doi.org/10.1134/s0006297906120078

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[Untitled]

Autor: R. I. Gvozdev, I. A. Tukhvatullin, K. K. Andersson

Publikováno v: Russian Chemical Bulletin. 50:1867-1876

Computer analysis of a wide range of primary sequences showed that α-, β-, and γ-peptides of membrane-bound methane hydroxylase contained 2, 7, and 6 transmembrane helices respectively. Conservative amino acid residues participating in complex for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b4f29c6b42c2ae48c768774d3440c769
https://doi.org/10.1023/a:1014342431711

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Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases

Autor: R. I. Gvozdev, A. R. Gvozdev, I. A. Tukhvatullin

Publikováno v: Biochemistry. Biokhimiia. 77(8)

This review considers quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases, enzymes that are present in numerous methylotrophic eu- and prokaryotes and significantly differ in their primary and quaternary structure. The cofacto

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8836bb16703f80b32e8d8bb81e8ff89c
https://pubmed.ncbi.nlm.nih.gov/22860906

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Purification and properties of alcohol oxidase from Pichia putida

Autor: I. A. Tukhvatullin, A. R. Gvozdev, R. I. Gvozdev

Publikováno v: Biochemistry. Biokhimiia. 75(2)

Alcohol oxidase (AO) was extracted from the methylotrophic yeast Pichia putida and purified using various methods. AO purified by crystallization was homogeneous based on analytical centrifugation with subsequent gel filtration and SDS-PAGE. The mole

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d54ce93af08d6019f6fa95b70e740b0
https://pubmed.ncbi.nlm.nih.gov/20367612

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[Purification and properties of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M)]

Autor: R I, Gvozdev, I A, Tukhvatullin, L V, Tumanova

Publikováno v: Izvestiia Akademii nauk. Seriia biologicheskaia. (2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fb78bb2d7b46432def0ff146ced03932
https://pubmed.ncbi.nlm.nih.gov/18946992

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[The binuclear iron site of the membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M)]

Autor: L. V. Tumanova, D. Sh. Burbaev, K. K. Andersson, I. A. Tukhvatullin, R. I. Gvozdev

Publikováno v: Bioorganicheskaia khimiia. 34(2)

The particulate membrane-bound methane hydroxylase (pMMOH) was isolated from methane-oxidizing cells of Methylococcus capsulatus (strain M). At SDS PAGE, pMMOH displays three bands: 47 (alpha), 27 (beta), and 25 kDa (gamma). The ESR spectrum of pMMOH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48d646cc3d36e25532af82f929ca3ab6
https://pubmed.ncbi.nlm.nih.gov/18522275

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The structure of the active center of beta-peptide membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus bath

Autor: I A, Tukhvatullin, R I, Gvozdev, K K, Andersson

Publikováno v: Doklady biochemistry : proceedings of the Academy of Sciences of the USSR, Biochemistry section. 374(1-6)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ba3ef2f0375d7bd668840b32336ba4f2
https://pubmed.ncbi.nlm.nih.gov/11109958

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