Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Brian J. Brazeau"'
Publikováno v:
Biochemical and Biophysical Research Communications. 338:254-261
EPR spin-trapping experiments were carried out using the three-component soluble methane monooxygenase (MMO). Spin-traps 5,5-dimethyl-1-pyrroline N-oxide (DMPO), α-4-pyridyl-1-oxide N-tert-butylnitrone (POBN), and nitrosobenzene (NOB) were used to i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dc5c0aa07b4b52b022647a1b712ab8b
https://doi.org/10.1016/j.bbrc.2005.08.216
https://doi.org/10.1016/j.bbrc.2005.08.216
Publikováno v:
Archives of Biochemistry and Biophysics. 428:22-31
This review will focus on how X-ray crystallographic studies of copper-containing amine oxidases have complemented the solution, kinetic, and spectroscopic research on this ubiquitous class of enzymes. These enzymes not only contain a copper ion at t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04258870ac616907f4878609b0dd1820
https://doi.org/10.1016/j.abb.2004.03.034
https://doi.org/10.1016/j.abb.2004.03.034
Publikováno v:
Biochemical and Biophysical Research Communications. 312:143-148
Effector proteins alter the kinetic or catalytic course of many oxygenase reactions. One of the first oxygenase effectors to be described was putidaredoxin, which serves to gate electron transfer into oxy-P450cam. In the nonheme, methane monooxygenas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16e139c716b52c8b0daf7a0360af7274
https://doi.org/10.1016/j.bbrc.2003.09.242
https://doi.org/10.1016/j.bbrc.2003.09.242
Autor:
Brian J. Brazeau, John D. Lipscomb
Publikováno v:
Biochemistry. 42:5618-5631
The regulatory component MMOB of soluble methane monooxygenase (sMMO) has been hypothesized to control access of substrates into the active site of the hydroxylase component (MMOH) through formation of a size specific channel or region of increased s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5d86dd594202ccdac5da8026b40d409
https://doi.org/10.1021/bi027429i
https://doi.org/10.1021/bi027429i
Publikováno v:
International Congress Series. 1233:205-212
Methane monooxygenase (MMO) catalyzes the NADH and O2 coupled oxidation of CH4 to yield CH3OH. The enzyme consists of three components: MMOH (hydroxylase), MMOB (effector), and MMOR (reductase). We have structurally characterized MMOH and MMOB. The a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9abd65d61400de9d73e5be682846e085
https://doi.org/10.1016/s0531-5131(02)00278-9
https://doi.org/10.1016/s0531-5131(02)00278-9
Autor:
Brian J. Brazeau, John D. Lipscomb
Publikováno v:
International Congress Series. 1233:229-233
Methane monooxygenase (MMO) contains a binuclear iron cluster that forms a bis-μ-oxo Fe(IV)2 intermediate termed compound Q (Q) which has previously been shown to be the species that oxidizes methane to form methanol. This report summarizes the resu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f354b090627a0fb2e2cfb20f6f82138d
https://doi.org/10.1016/s0531-5131(02)00145-0
https://doi.org/10.1016/s0531-5131(02)00145-0
Publikováno v:
Journal of the American Chemical Society. 123:11831-11837
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=doi_________::972f2ac881ec719b4e1676c548ce1d83
https://doi.org/10.1021/ja016376+
https://doi.org/10.1021/ja016376+
Publikováno v:
Biochemistry. 47(32)
The multicomponent soluble form of methane monooxygenase (sMMO) catalyzes the oxidation of methane through the activation of O 2 at a nonheme biferrous center in the hydroxylase component, MMOH. Reactivity is limited without binding of the sMMO effec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1e0ff4b5d9624d3aa526c36880af12d
https://pubmed.ncbi.nlm.nih.gov/18627173
https://pubmed.ncbi.nlm.nih.gov/18627173
Autor:
John D. Lipscomb, Brian J. Brazeau
Publikováno v:
Biochemistry. 39(44)
The transient kinetics of formation and decay of the reaction cycle intermediates of the Methylosinus trichosporium OB3b methane monooxygenase (MMO) catalytic cycle are studied as a function of temperature and substrate type and deuteration. Kinetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::212a22fe5100c1a5fa0bce7c3bdddb83
https://pubmed.ncbi.nlm.nih.gov/11063587
https://pubmed.ncbi.nlm.nih.gov/11063587
Autor:
Brian J. Brazeau, John D. Lipscomb
Publikováno v:
Subcellular Biochemistry ISBN: 9780306463990
Dioxygen is a unique reagent for biological systems being at once thermodynamically reactive and kinetically stable. Life in a sea of oxygen is possible because oxygenase and oxidase enzymes have evolved that allow the inherent reactivity of dioxygen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5956deef12fc01bce3f91f4dbfda32c2
https://doi.org/10.1007/0-306-46828-x_7
https://doi.org/10.1007/0-306-46828-x_7
