Journal article
Authors list: SORGENFREI, O; LINDER, D; KARAS, M; KLEIN, A
Publication year: 1993
Pages: 1355-1358
Journal: European Journal of Biochemistry
Volume number: 213
Issue number: 3
ISSN: 0014-2956
Open access status: Bronze
DOI Link: https://doi.org/10.1111/j.1432-1033.1993.tb17888.x
Publisher: Wiley: 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 style: SORGENFREI, 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 style: SORGENFREI, 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