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Carboxy‐terminal processing of the large subunit of [NiFe] hydrogenases
Author(s) -
Me Nanda K.,
Robbins Jeff,
Der Vartanian Marie,
Patil Daulat,
Peck Harry D.,
Me Angeli L.,
Robson Robert L.,
Przybyla Alan E.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80303-c
Subject(s) - hydrogenase , periplasmic space , protein subunit , biochemistry , amino acid , peptide sequence , desulfovibrio , chemistry , enzyme , biology , bacteria , escherichia coli , gene , genetics
Two electrophoretic forms of the large subunit of the soluble periplasmic [NiFe] hydrogenase from Desulfovibrio gigas have been detected by Western analysis. The faster moving form co‐migrates with the large subunit from purified, active enzyme. Amino acid sequence and composition of the C‐terminal tryptic peptide of the large subunit from purified hydrogenase revealed that it is 15 amino acids shorter than that predicted by the nucleotide sequence. Processing of the nascent large subunit occurs by C‐terminal cleavage between His 536 and Val 537 , residues which are highly conserved among [NiFe] hydrogenases. Mutagenesis of the analogous residues, His 582 and Val 583 , in the E. coli hydrogenase‐1 (HYD1) large subunit resulted in significant decrease in processing and HYD1 activity.