Journal article

A NOVEL VERY SMALL SUBUNIT OF A SELENIUM-CONTAINING [NIFE] HYDROGENASE OF METHANOCOCCUS-VOLTAE IS POSTTRANSLATIONALLY PROCESSED BY CLEAVAGE AT A DEFINED POSITION


Authors listSORGENFREI, O; LINDER, D; KARAS, M; KLEIN, A

Publication year1993

Pages1355-1358

JournalEuropean Journal of Biochemistry

Volume number213

Issue number3

ISSN0014-2956

Open access statusBronze

DOI Linkhttps://doi.org/10.1111/j.1432-1033.1993.tb17888.x

PublisherWiley: No OnlineOpen


Abstract
A coenzyme-F420 non-reducing [NiFe] hydrogenase was isolated from Methanococcus voltae. It consists of three subunits. They are the products of the previously identified genes vhuA, vhuG and vhuU. The vhuU gene product is of only 25 amino acids. This novel very small hydrogenase subunit contains selenocysteine within a conserved amino-acid sequence previously shown to be involved in Ni coordination. The subunit is shorter than the predicted primary gene product and is therefore apparently post-translationally processed.



Citation Styles

Harvard Citation styleSORGENFREI, O., LINDER, D., KARAS, M. and KLEIN, A. (1993) A NOVEL VERY SMALL SUBUNIT OF A SELENIUM-CONTAINING [NIFE] HYDROGENASE OF METHANOCOCCUS-VOLTAE IS POSTTRANSLATIONALLY PROCESSED BY CLEAVAGE AT A DEFINED POSITION, European Journal of Biochemistry, 213(3), pp. 1355-1358. https://doi.org/10.1111/j.1432-1033.1993.tb17888.x

APA Citation styleSORGENFREI, O., LINDER, D., KARAS, M., & KLEIN, A. (1993). A NOVEL VERY SMALL SUBUNIT OF A SELENIUM-CONTAINING [NIFE] HYDROGENASE OF METHANOCOCCUS-VOLTAE IS POSTTRANSLATIONALLY PROCESSED BY CLEAVAGE AT A DEFINED POSITION. European Journal of Biochemistry. 213(3), 1355-1358. https://doi.org/10.1111/j.1432-1033.1993.tb17888.x


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