Zobrazeno 1 - 10 of 47 pro vyhledávání: '"J. D. Lipscomb"'
2
Intermediate Q from soluble methane monooxygenase hydroxylates the mechanistic substrate probe norcarane: evidence for a stepwise reaction
Autor: B J, Brazeau, R N, Austin, C, Tarr, J T, Groves, J D, Lipscomb
Publikováno v: Journal of the American Chemical Society. 123(48)
Norcarane is a valuable mechanistic probe for enzyme-catalyzed hydrocarbon oxidation reactions because different products or product distributions result from concerted, radical, and cation based reactions. Soluble methane monooxygenase (sMMO) from M
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d9d9a27a8644a12618213c34fb56e5ae
https://pubmed.ncbi.nlm.nih.gov/11724588
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4
Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K. EPR evidence for conformational change upon reduction or binding of component B to the diferric state
Autor: A, Davydov, R, Davydov, A, Gräslund, J D, Lipscomb, K K, Andersson
Publikováno v: The Journal of biological chemistry. 272(11)
The soluble form of methane monooxygenase (MMO) consists of three components: reductase, hydroxylase (MMOH), and "B" (MMOB). Resting MMOH contains a diferric bis-mu-hydroxodinuclear iron "diamond core" cluster which is the site of oxygen activation c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::477fe8d2519a10601531fccffc674ecf
https://pubmed.ncbi.nlm.nih.gov/9054392
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5
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b
Autor: N, Elango, R, Radhakrishnan, W A, Froland, B J, Wallar, C A, Earhart, J D, Lipscomb, D H, Ohlendorf
Publikováno v: Protein science : a publication of the Protein Society. 6(3)
Methane monooxygenase (MMO), found in aerobic methanotrophic bacteria, catalyzes the O2-dependent conversion of methane to methanol. The soluble form of the enzyme (sMMO) consists of three components: a reductase, a regulatory "B" component (MMOB), a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7490ded22ca683af3378ca6273e9cc8d
https://pubmed.ncbi.nlm.nih.gov/9070438
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6
Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity
Autor: M A, Miller, J D, Lipscomb
Publikováno v: The Journal of biological chemistry. 271(10)
Homoprotocatechuate 2,3-dioxygenase (2,3-HPCD) cleaves the aromatic ring of its substrate with insertion of both atoms of oxygen from O2 to form alpha-hydroxy- delta-carboxymethyl cis-muconic semialdehyde. The enzyme has been purified from the Gram-p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d54ba516530a6acb7906f0d47b479d8f
https://pubmed.ncbi.nlm.nih.gov/8621411
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7
Transient intermediates of the methane monooxygenase catalytic cycle
Autor: S K, Lee, J C, Nesheim, J D, Lipscomb
Publikováno v: The Journal of biological chemistry. 268(29)
Three new intermediates of the catalytic cycle of the soluble form of methane monooxygenase (MMO) isolated from Methylosinus trichosporium OB3b have been detected using transient kinetic techniques. MMO consists of hydroxylase (MMOH), reductase, and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e945a4766a29403eb0b38143ce909929
https://pubmed.ncbi.nlm.nih.gov/8408008
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8
Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase
Autor: A M, Orville, J D, Lipscomb
Publikováno v: The Journal of biological chemistry. 268(12)
The active site Fe3+ of protocatechuate (PCA) 3,4-dioxygenase can be nonenzymatically reduced to Fe2+, to give a colorless and EPR-silent enzyme (Er). Nitric oxide (NO) binds to Er to yield a species with EPR (S = 3/2; g = 4.341, 3.693, 1.984; E/D =
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3221e72cb722d790f6f9af2a73d1e08
https://pubmed.ncbi.nlm.nih.gov/8386164
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9
Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. A novel role for protein-protein interactions in an oxygenase mechanism
Autor: W A, Froland, K K, Andersson, S K, Lee, Y, Liu, J D, Lipscomb
Publikováno v: The Journal of biological chemistry. 267(25)
The soluble methane monooxygenase (MMO) system, consisting of reductase, component B, and hydroxylase (MMOH), catalyzes NADH and O2-dependent monooxygenation of many hydrocarbons. MMOH contains 2 mu-(H or R)oxo-bridged dinuclear iron clusters thought
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1788b36b864021e22c8b32aeeff39d02
https://pubmed.ncbi.nlm.nih.gov/1325441
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10
Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes
Autor: A M, Orville, V J, Chen, A, Kriauciunas, M R, Harpel, B G, Fox, E, Münck, J D, Lipscomb
Publikováno v: Biochemistry. 31(19)
Isopenicillin N synthase (IPNS) catalyzes double ring closure of the tripeptide (L-alpha-amino-delta-adipoyl)-L-cysteinyl-D-valine (ACV) to form the beta-lactam and thiazolidine rings of penicillin-type antibiotics. Our previous spectroscopic study u
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::904fd6d06b48f9b331043f4ff8ce8da0
https://pubmed.ncbi.nlm.nih.gov/1316153
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