Linked Life Data

3651442

Source:http://linkedlifedata.com/resource/pubmed/id/3651442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1987-11-16
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4139-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Redox properties of the quinoprotein methylamine dehydrogenase from paracoccus denitrificans.
pubmed:affiliation
Molecular Biology Division, Veterans Administration Medical Center, San Francisco, California 94121.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't