Výsledky vyhledávání - "S W, Ragsdale"

Autor: S W, Ragsdale

Publikováno v: Current Opinion in Chemical Biology. 2:208-215

Significant advances have been made in the past year in our understanding of the structure, function, and mode of regulation and assembly of nickel-containing enzymes. The highlight of 1997 was the elucidation of the methyl-CoM reductase structure.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c5578fcc1e85db705b1963a10f0e138
https://doi.org/10.1016/s1367-5931(98)80062-8

Zobrazit plný text záznamu

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: S. W. Ragsdale, Wei-Ping Lu, Peter E. Jablonski, James G. Ferry

Publikováno v: Journal of Biological Chemistry. 268:325-329

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aebe5224ca444d57de5f9423f1775ada
https://doi.org/10.1016/s0021-9258(18)54153-3

Zobrazit plný text záznamu

Evidence for intersubunit communication during acetyl-CoA cleavage by the multienzyme CO dehydrogenase/acetyl-CoA synthase complex from Methanosarcina thermophila. Evidence that the beta subunit catalyzes C-C and C-S bond cleavage

Autor: E, Murakami, S W, Ragsdale

Publikováno v: The Journal of biological chemistry. 275(7)

The carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) from Methanosarcina thermophila is part of a five-subunit complex consisting of alpha, beta, gamma, delta, and epsilon subunits. The multienzyme complex catalyzes the reversible oxidati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e37535f68cf48ace4e7d0d207f5fa1f3
https://pubmed.ncbi.nlm.nih.gov/10671500

Zobrazit plný text záznamu

The role of an iron-sulfur cluster in an enzymatic methylation reaction. Methylation of CO dehydrogenase/acetyl-CoA synthase by the methylated corrinoid iron-sulfur protein

Autor: S, Menon, S W, Ragsdale

Publikováno v: The Journal of biological chemistry. 274(17)

This paper focuses on how a methyl group is transferred from a methyl-cobalt(III) species on one protein (the corrinoid iron-sulfur protein (CFeSP)) to a nickel iron-sulfur cluster on another protein (carbon monoxide dehydrogenase/acetyl-CoA synthase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e13450e632d96e52df68292f009a059c
https://pubmed.ncbi.nlm.nih.gov/10206956

Zobrazit plný text záznamu

Characterization of the iron-sulfur clusters in ferredoxin from acetate-grown Methanosarcina thermophila

Autor: Wei-Ping Lu, James G. Ferry, S. W. Ragsdale, A. P. Clements, L. Kilpatrick

Publikováno v: Journal of bacteriology. 176(9)

Ferredoxin from Methanosarcina thermophila is an electron acceptor for the CO dehydrogenase complex which decarbonylates acetyl-coenzyme A and oxidizes the carbonyl group to carbon dioxide in the pathway for conversion of the methyl group of acetate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b377f3ded230d9fc26b782e3f795aaa
https://pubmed.ncbi.nlm.nih.gov/8169218

Zobrazit plný text záznamu

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::21c7b199e4af8cc7a67d780074b9758e
https://pubmed.ncbi.nlm.nih.gov/8144565

Zobrazit plný text záznamu

Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity

Autor: W P, Lu, I, Schiau, J R, Cunningham, S W, Ragsdale

Publikováno v: The Journal of biological chemistry. 268(8)

The corrinoid/iron-sulfur protein (C/Fe-SP) from Clostridium thermoaceticum acts as a methyl group carrier in the anaerobic acetyl-CoA pathway of CO and CO2 fixation. Consisting of a small (approximately 33 kDa) and a large (approximately 55 kDa) sub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8a83d2532fcfc5c453ba526c04a9709c
https://pubmed.ncbi.nlm.nih.gov/8449924

Zobrazit plný text záznamu

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)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ddb9d3f19c4282a75c8250255c4929f3
https://pubmed.ncbi.nlm.nih.gov/8380157

Zobrazit plný text záznamu

The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum

Autor: T A, Morton, J A, Runquist, S W, Ragsdale, T, Shanmugasundaram, H G, Wood, L G, Ljungdahl

Publikováno v: The Journal of biological chemistry. 266(35)

CO dehydrogenase/acetyl-coenzyme A synthase (CODH) is the central enzyme in the pathway of acetyl-coenzyme A biosynthesis in Clostridium thermoaceticum. It catalyzes the interconversion of CO and CO2 and the synthesis of acetyl-coenzyme A from the me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::50d7fa89a407c699a99bda1792bf4d96
https://pubmed.ncbi.nlm.nih.gov/1748656

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání