The two subunits of the nickel-iron hydrogenase from Desulfovibrio gigas have been purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and their amino acid compositions have been determined. The N-terminal sequences for 15 residues of the large subunit (Mr 62,000) and 25 residues of the small subunit (Mr 26,000), respectively, were established. The occurrence of several cysteine residues in the small subunit is discussed in relation with their possible role in the binding of the redox centers of the enzyme.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The two subunits of the nickel-iron hydrogenase from Desulfovibrio gigas have been purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and their amino acid compositions have been determined. The N-terminal sequences for 15 residues of the large subunit (Mr 62,000) and 25 residues of the small subunit (Mr 26,000), respectively, were established. The occurrence of several cysteine residues in the small subunit is discussed in relation with their possible role in the binding of the redox centers of the enzyme.
|
| skos:exactMatch | |
| uniprot:name |
Biochimie
|
| uniprot:author |
Bonicel J.,
Bovier-Lapierre G.E.,
Forget N.,
Hatchikian C.,
Niviere V.
|
| uniprot:date |
1988
|
| uniprot:pages |
267-272
|
| uniprot:title |
Isolation, amino acid analysis and N-terminal sequence determination of the two subunits of the nickel-containing hydrogenase of Desulfovibrio gigas.
|
| uniprot:volume |
70
|
| dc-term:identifier |
doi:10.1016/0300-9084(88)90070-3
|