Výsledky vyhledávání - "A. 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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The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)

Autor: H H, Nguyen, A K, Shiemke, S J, Jacobs, B J, Hales, M E, Lidstrom, S I, Chan

Publikováno v: The Journal of biological chemistry. 269(21)

It is shown that the particulate methane monooxygenase (pMMO) has an obligate requirement for copper. The MMO activity in the particulate fractions obtained from Methylococcus capsulatus (Bath) cells is found to increase with increasing copper conten

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9a86c4df7012d9631b8ec7ddaccabe53
https://pubmed.ncbi.nlm.nih.gov/8195135

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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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