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Primary structure of protein B from Pseudomonas putida , member of a new class of 2Fe‐2S ferredoxins
Author(s) -
Morrice Nicholas,
Geary Philip,
Cammack Richard,
Harris Alan,
Beg Fatima,
Aitken Alastair
Publication year - 1988
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(88)80845-7
Subject(s) - ferredoxin , pseudomonas putida , protein primary structure , peptide sequence , biochemistry , chemistry , cysteine , stereochemistry , biology , enzyme , gene
The primary structure of the 2Fe‐2S ferredoxin (protein B) from the benzene dioxygenase system of Pseudomonas putida strain NCIB 12190 was determined by gas‐phase sequencing of the protein and its fragments. Fast atom bombardment mass spectrometry indicated a molecular mass of 11860 Da. The sequence contained five cysteine residues, four of which would be required to coordinate the iron‐sulphur cluster. The amino acid sequence determined in the present study is compared to that of a protein deduced from the DNA sequence from another strain of Pseudomonas putida . Little sequence homology was observed when protein B was compared to 2Fe‐2S ferredoxins from plant and cyanobacterial sources. The novel sequence determined here suggests a new class of ferredoxin, which is consistent with the observed mid‐point redox potential being significantly less negative ( −155 mV) than those of the 2Fe‐2S ferredoxins involved in photosynthesis (−310 to −455 mV)