rdf:type |
|
lifeskim:mentions |
umls-concept:C0004611,
umls-concept:C0006675,
umls-concept:C0013846,
umls-concept:C0020275,
umls-concept:C0038720,
umls-concept:C0038750,
umls-concept:C0301630,
umls-concept:C0337112,
umls-concept:C0392756,
umls-concept:C0995408,
umls-concept:C1514873,
umls-concept:C1524075,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
|
pubmed:issue |
1
|
pubmed:dateCreated |
1991-11-21
|
pubmed:abstractText |
Calcium is found a strong stimulator of sulfite reduction from hydrogen. A coupling protein of molecular weight 65,000 can be isolated from Desulfovibrio gigas. It functions in a reconstituted electron transfer chain between hydrogenase and sulfite reductase. Its N-terminal sequence shows high homologies with calcium or magnesium binding sites from other calcium-binding proteins.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
180
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
238-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1930220-Amino Acid Sequence,
pubmed-meshheading:1930220-Bacterial Proteins,
pubmed-meshheading:1930220-Calcium,
pubmed-meshheading:1930220-Calmodulin,
pubmed-meshheading:1930220-Carrier Proteins,
pubmed-meshheading:1930220-Desulfovibrio,
pubmed-meshheading:1930220-Electron Transport,
pubmed-meshheading:1930220-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1930220-Hydrogen,
pubmed-meshheading:1930220-Hydrogenase,
pubmed-meshheading:1930220-Molecular Sequence Data,
pubmed-meshheading:1930220-Molecular Weight,
pubmed-meshheading:1930220-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:1930220-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1930220-Sulfites
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pubmed:year |
1991
|
pubmed:articleTitle |
Calcium is required for the reduction of sulfite from hydrogen in a reconstituted electron transfer chain from the sulfate reducing bacterium, Desulfovibrio gigas.
|
pubmed:affiliation |
Department of Biochemistry, University of Georgia, Athens 30602.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|