| pubmed-article:3223938 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3223938 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:3223938 | lifeskim:mentions | umls-concept:C0077173 | lld:lifeskim |
| pubmed-article:3223938 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3223938 | pubmed:dateCreated | 1989-3-16 | lld:pubmed |
| pubmed-article:3223938 | pubmed:abstractText | Trimethylamine dehydrogenase, which contains one covalently bound 6-S-cysteinyl-FMN and one Fe4S4 cluster per subunit of molecular mass 83,000 Da, was purified to homogeneity from the methylotrophic bacterium W3A1. Microcoulometry at pH 7 in 50 mM-Mops buffer containing 0.1 mM-EDTA and 0.1 M-KCl revealed that the native enzyme required the addition of 3 reducing equivalents per subunit for complete reduction. In contrast, under identical conditions the phenylhydrazine-inhibited enzyme required the addition of 0.9 reducing equivalent per subunit with a midpoint potential of +110 mV. Least-squares analysis of the microcoulometric data obtained for the native enzyme, assuming uptake of 1 electron by Fe4S4 and 2 electrons by FMN, indicated midpoint potentials of +44 mV and +36 mV for the FMN/FMN.- and FMN.-/FMNH2 couples respectively and +102 mV for reduction of the Fe4S4 cluster. | lld:pubmed |
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| pubmed-article:3223938 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3223938 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3223938 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3223938 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3223938 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3223938 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3223938 | pubmed:author | pubmed-author:BarberM JMJ | lld:pubmed |
| pubmed-article:3223938 | pubmed:author | pubmed-author:SpenceJ TJT | lld:pubmed |
| pubmed-article:3223938 | pubmed:author | pubmed-author:PollockVV | lld:pubmed |
| pubmed-article:3223938 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3223938 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3223938 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:3223938 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3223938 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3223938 | pubmed:pagination | 657-9 | lld:pubmed |
| pubmed-article:3223938 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3223938 | pubmed:meshHeading | pubmed-meshheading:3223938-... | lld:pubmed |
| pubmed-article:3223938 | pubmed:meshHeading | pubmed-meshheading:3223938-... | lld:pubmed |
| pubmed-article:3223938 | pubmed:meshHeading | pubmed-meshheading:3223938-... | lld:pubmed |
| pubmed-article:3223938 | pubmed:meshHeading | pubmed-meshheading:3223938-... | lld:pubmed |
| pubmed-article:3223938 | pubmed:meshHeading | pubmed-meshheading:3223938-... | lld:pubmed |
| pubmed-article:3223938 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3223938 | pubmed:articleTitle | Microcoulometric analysis of trimethylamine dehydrogenase. | lld:pubmed |
| pubmed-article:3223938 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of South Florida, College of Medicine, Tampa 33612. | lld:pubmed |
| pubmed-article:3223938 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3223938 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3223938 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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