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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-4-16
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pubmed:abstractText |
Rubredoxin and desulforedoxin both contain an Fe(S-Cys)4 center. However, the spectroscopic properties of the center in desulforedoxin differ from rubredoxin. These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated highspin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
231
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
679-82
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9070870-Cysteine,
pubmed-meshheading:9070870-Desulfovibrio,
pubmed-meshheading:9070870-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:9070870-Iron-Sulfur Proteins,
pubmed-meshheading:9070870-Mass Spectrometry,
pubmed-meshheading:9070870-Mutagenesis, Site-Directed,
pubmed-meshheading:9070870-Rubredoxins,
pubmed-meshheading:9070870-Spectrophotometry, Ultraviolet
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pubmed:year |
1997
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pubmed:articleTitle |
Conversion of desulforedoxin into a rubredoxin center.
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pubmed:affiliation |
Section of Hematology Research, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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