Abstract:
: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.
journal_name
Biochimiejournal_title
Biochimieauthors
Nivière V,Forget N,Bovier-Lapierre G,Bonicel J,Hatchikian Cdoi
10.1016/0300-9084(88)90070-3subject
Has Abstractpub_date
1988-02-01 00:00:00pages
267-72issue
2eissn
0300-9084issn
1638-6183pii
0300-9084(88)90070-3journal_volume
70pub_type
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