| pubmed-article:3651442 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3651442 | lifeskim:mentions | umls-concept:C0030411 | lld:lifeskim |
| pubmed-article:3651442 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:3651442 | lifeskim:mentions | umls-concept:C0066319 | lld:lifeskim |
| pubmed-article:3651442 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3651442 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:3651442 | pubmed:dateCreated | 1987-11-16 | lld:pubmed |
| pubmed-article:3651442 | pubmed:abstractText | Paracoccus denitrificans synthesizes a methylamine dehydrogenase that contains a covalently bound form of pyrroloquinoline quinone as a prosthetic group [Husain, M., & Davison, V.L. (1987) J. Bacteriol. 169, 1712-1717]. Anaerobic reductive titration of this enzyme with dithionite proceeded through a semiquinone intermediate with spectral properties quite distinct from those of the oxidized and reduced species. From these data the molar extinction coefficients were calculated at various wavelengths for the three redox states of this enzyme. The semiquinone was slowly reoxidized under aerobic conditions. The fully reduced enzyme was stable in the presence of oxygen and slowly reoxidized by ferricyanide. Reductive titration of methylamine dehydrogenase with methylamine proceeded directly to the fully reduced form of the enzyme without detectable formation of the semiquinone. Electrochemical titrations of the enzyme yielded an overall midpoint potential value for the two-electron couple (fully oxidized/fully reduced) of 100 +/- 4 mV and an n value of 2.15 +/- 0.15. | lld:pubmed |
| pubmed-article:3651442 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3651442 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3651442 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3651442 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3651442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3651442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3651442 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3651442 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3651442 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:3651442 | pubmed:author | pubmed-author:KnaffD BDB | lld:pubmed |
| pubmed-article:3651442 | pubmed:author | pubmed-author:HusainMM | lld:pubmed |
| pubmed-article:3651442 | pubmed:author | pubmed-author:DavidsonV LVL | lld:pubmed |
| pubmed-article:3651442 | pubmed:author | pubmed-author:GrayK AKA | lld:pubmed |
| pubmed-article:3651442 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3651442 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:3651442 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:3651442 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3651442 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3651442 | pubmed:pagination | 4139-43 | lld:pubmed |
| pubmed-article:3651442 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:meshHeading | pubmed-meshheading:3651442-... | lld:pubmed |
| pubmed-article:3651442 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3651442 | pubmed:articleTitle | Redox properties of the quinoprotein methylamine dehydrogenase from paracoccus denitrificans. | lld:pubmed |
| pubmed-article:3651442 | pubmed:affiliation | Molecular Biology Division, Veterans Administration Medical Center, San Francisco, California 94121. | lld:pubmed |
| pubmed-article:3651442 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3651442 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3651442 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:3651442 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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