Výsledky vyhledávání

The β and γ Classes of Carbonic Anhydrase

Autor: S A Zimmerman, J G Ferry

Publikováno v: Current Pharmaceutical Design. 14:716-721

There are currently five (alpha, beta, gamma, delta, zeta) classes of carbonic anhydrases (CA's) of which the alpha-class from mammalian sources has been studied to a much greater extent compared to the other four classes. Yet, CA's other than the al

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https://doi.org/10.2174/138161208783877929

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CO DEHYDROGENASE

Autor: J G, Ferry

Publikováno v: Annual Review of Microbiology. 49:305-333

Structurally and functionally diverse CO dehydrogenases are key components of various energy-yielding pathways in aerobic and anaerobic microbes from the Bacteria and Archaea domains. Aerobic microbes utilize Mo-Fe-flavin CO dehydrogenases to oxidize

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c2fa069b72d7994b6639fae81e07e2c
https://doi.org/10.1146/annurev.mi.49.100195.001513

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Formate dehydrogenase

Autor: J G, Ferry

Publikováno v: FEMS Microbiology Letters. 87:377-382

Formate is a substrate, or product, of diverse reactions catalyzed by eukaryotic organisms, eubacteria, and archaebacteria. A survey of metabolic groups reveals that formate is a common growth substrate, especially among the anaerobic eubacteria and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c73a454a4ccdb56a06c1175874c7e628
https://doi.org/10.1111/j.1574-6968.1990.tb04940.x

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Archaeal proteasomes

Autor: R D, Barber, J G, Ferry

Publikováno v: Methods in enzymology. 330

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a154ef6625c925cf3648a94892d168f8
https://pubmed.ncbi.nlm.nih.gov/11210520

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Characterization of the metal centers of the Ni/Fe-S component of the carbon-monoxide dehydrogenase enzyme complex from Methanosarcina thermophila

Autor: W P, Lu, P E, Jablonski, M, Rasche, J G, Ferry, S W, Ragsdale

Publikováno v: The Journal of biological chemistry. 269(13)

Methanosarcina thermophila contains a multienzyme complex called the carbon-monoxide dehydrogenase complex, which has been resolved into a nickel/iron-sulfur and a corrinoid/iron-sulfur component. This complex plays a central role in acetoclastic met

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https://pubmed.ncbi.nlm.nih.gov/8144565

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Characterization of the metal centers of the corrinoid/iron-sulfur component of the CO dehydrogenase enzyme complex from Methanosarcina thermophila by EPR spectroscopy and spectroelectrochemistry

Autor: P E, Jablonski, W P, Lu, S W, Ragsdale, J G, Ferry

Publikováno v: The Journal of biological chemistry. 268(1)

The multienzyme carbon monoxide dehydrogenase complex from Methanosarcina thermophila contains at least two protein components: a CO-oxidizing nickel/iron-sulfur (Ni/Fe-S) component and a cobalt-containing corrinoid/iron-sulfur component (Co/Fe-S). T

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https://pubmed.ncbi.nlm.nih.gov/8380157

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Reductive dechlorination of trichloroethylene by the CO-reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila

Autor: P E, Jablonski, J G, Ferry

Publikováno v: FEMS microbiology letters. 75(1)

Trichloroethylene (TCE) was reductively dechlorinated to cis-dichloroethylene, trans-dichloroethylene, 1,1-dichloroethylene, vinyl chloride, and ethylene by the CO-reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila; the apparent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c6d50a1a9fd4b293b3c67d2f3199a9aa
https://pubmed.ncbi.nlm.nih.gov/1526465

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Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Autor: J L, Johnson, N R, Bastian, N L, Schauer, J G, Ferry, K V, Rajagopalan

Publikováno v: FEMS microbiology letters. 61(2-3)

The pterin cofactor in formate dehydrogenase isolated from Methanobacterium formicium is identified as molybdopterin guanine dinucleotide. The pterin, stabilized as the alkylated, dicarboxamidomethyl derivative, is shown to have absorption and chroma

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https://pubmed.ncbi.nlm.nih.gov/2037231

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Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila

Autor: K C, Terlesky, J G, Ferry

Publikováno v: The Journal of biological chemistry. 263(9)

Cell extracts from acetate-grown Methanosarcina thermophila contained CO-oxidizing:H2-evolving activity 16-fold greater than extracts from methanol-grown cells. Following fractionation of cell extracts into soluble and membrane components, CO-depende

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https://pubmed.ncbi.nlm.nih.gov/3279028

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