Výsledky vyhledávání - "Andrew K. Shiemke"

Inhibition of Membrane-Bound Methane Monooxygenase and Ammonia Monooxygenase by Diphenyliodonium: Implications for Electron Transfer

Autor: Luis A. Sayavedra-Soto, Daniel J. Arp, Andrew K. Shiemke

Publikováno v: Journal of Bacteriology. 186:928-937

Diphenyliodonium (DPI) is known to irreversibly inactivate flavoproteins. We have found that DPI inhibits both membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO) of Nitrosomonas europaea . The ef

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::058642009101c7dade136cad1e3b9fb1
https://doi.org/10.1128/jb.186.4.928-937.2004

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Evidence that copper is a required cofactor for the membrane-bound form of methane monooxygenase

Autor: Andrew K. Shiemke, Scott A. Cook

Publikováno v: Journal of Inorganic Biochemistry. 63:273-284

The membrane bound enzyme methane monooxygenase (pMMO) is a mixed function oxygenase that initiates the oxidative metabolism of methane in methanotrophic bacteria. In this paper, we show that copper is required for catalytic activity of pMMO. Additio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2fab92da289e9b5b20f74af656580c3
https://doi.org/10.1016/0162-0134(95)00239-1

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Cytochrome aa 3 from Methylococcus capsulatus (Bath)

Autor: Andrew K. Shiemke, Alan A. DiSpirito, Cinder L. Krema, Sean W. Jordan, James A. Zahn

Publikováno v: Archives of Microbiology. 161:258-265

A cytochrome aa 3-type oxidase was isolated with and without a c-type cytochrome (cytochrome c-557) from Methylococcus capsulatus Bath by ion-exchange and hydrophobic chromatography in the presence of Triton X-100. Although cytochrome c-557 was not a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c108ad34f6438fbbc7b6bbf382140e7f
https://doi.org/10.1007/bf00248702

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Resonance Raman study of oxyhemerythrin and hydroxomethemerythrin. Evidence for hydrogen bonding of ligands to the iron-oxygen-iron center

Autor: Andrew K. Shiemke, Joann Sanders-Loehr, Thomas M. Loehr

Publikováno v: Journal of the American Chemical Society. 108(9)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ac2d511ef3a8468dec057e0b58bc50e
https://pubmed.ncbi.nlm.nih.gov/22175597

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Trichloroethylene oxidation by the membrane-associated methane monooxygenase in type I, type II and type X methanotrophs

Autor: Jay Gulledge, J. Colin Murrell, Mary E. Lidstrom, Alan A. DiSpirito, Andrew K. Shiemke, Cinder L. Krema

Publikováno v: Biodegradation. 2:151-164

Trichloroethylene (TCE) oxidation was examined in 9 different methanotrophs grown under conditions favoring expression of the membrane associated methane monooxygenase. Depending on the strain, TCE oxidation rates varied from 1 to 677 pmol/min/mg cel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7de816b0cfa8787a9f027e2687abec08
https://doi.org/10.1007/bf00124489

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Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors

Autor: T. Miley, S.A. Cook, Andrew K. Shiemke, P. Singleton

Publikováno v: Archives of biochemistry and biophysics. 321(2)

Quinols can provide reducing equivalents for the membrane-bound form of methane monooxygenase (pMMO), substituting for NADH in whole cells and membranes. Furthermore, quinols are effective reductants for the detergent-solubilized enzyme, whereas NADH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8445f9b4e192a7763b0bb33ff5ec3cc9
https://pubmed.ncbi.nlm.nih.gov/7646068

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Spectroscopic characterization of heme A reconstituted myoglobin

Autor: Andrew K. Shiemke, Jason D. MacLeod, Siegfried M. Musser, Randy W. Larsen, Mark R. Ondrias, Sunney I. Chan, David J. Nunez, Hiep Hoa Nguyen

Publikováno v: Journal of inorganic biochemistry. 48(1)

The focus of this study was to examine the functional role of the unusual peripheral substitution of heme A. The effects of heme A stereochemistry on the reconstitution of the porphyrin have been examined in the heme A-apo-myoglobin complex using opt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e50d16651b523b46bf171ae44d7020db
https://pubmed.ncbi.nlm.nih.gov/1326598

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Quinols as electron donors for detergent solubilized and membrane-bound methane monooxygenase

Autor: Andrew K. Shiemke, T. Miley, S.A. Cook

Publikováno v: Journal of Inorganic Biochemistry. 59:385

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::02867b0a8395b4cf805c7e50b862eeaf
https://doi.org/10.1016/0162-0134(95)97483-7

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Methane monooxygenase: Copper content and spectroscopic properties of the membrane-bound form

Autor: Alan A. Dispirito, Andrew K. Shiemke, Sunney I. Chan, Mary E. Lidstrom

Publikováno v: Journal of Inorganic Biochemistry. 43:191

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::094f69f711cb1eba35002abc45538764
https://doi.org/10.1016/0162-0134(91)84183-a

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Raman spectroscopic evidence for side-on binding of peroxide ion to (ethylenediaminetetraacetato)ferrate(1-)

Autor: Thomas M. Loehr, Evan H. Appelman, John D. McCallum, Joann Sanders-Loehr, Andrew K. Shiemke, Salman Ahmad

Publikováno v: Inorganic Chemistry. 27:2230-2233

Resonance Raman spectra of the complex of Fe/sup III/-ethylenediaminetetraacetate with hydrogen peroxide have been obtained in the region of the peroxidic O-O stretching vibration that occurs at 815 cm/sup /minus/1/ in frozen solution. When the compl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2ebd97d5793741da2d82102074f60fd
https://doi.org/10.1021/ic00286a006

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