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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1985-5-20
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pubmed:abstractText |
Lys 109, Lys 112 and Glu 1 of cytochrome c2 from Rhodospirillum rubrum G-9 are about 4-fold less reactive towards acetic anhydride when cytochrome c2 is bound to the isolated photosynthetic reaction center from the same organism. The three shielded residues are clustered together on the "backside" of cytochrome c2. This contrasts with mitochondrial cytochrome c where "frontside" lysines are protected by different physiological electron transfer partners.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
16
|
pubmed:volume |
128
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
120-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2985069-Acetylation,
pubmed-meshheading:2985069-Chemistry, Physical,
pubmed-meshheading:2985069-Cytochrome c Group,
pubmed-meshheading:2985069-Cytochromes c2,
pubmed-meshheading:2985069-Electron Transport,
pubmed-meshheading:2985069-Physicochemical Phenomena,
pubmed-meshheading:2985069-Rhodospirillum rubrum,
pubmed-meshheading:2985069-Sodium Chloride
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pubmed:year |
1985
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pubmed:articleTitle |
Binding of cytochrome c2 to the isolated reaction center of Rhodospirillum rubrum involves the "backside" of cytochrome c2.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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