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Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli
Author(s) -
Lloyd Emma,
Mauk A.Grant
Publication year - 1994
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(94)80154-1
Subject(s) - myoglobin , recombinant dna , escherichia coli , chemistry , heme , escherichia , biochemistry , hemeprotein , nuclear magnetic resonance spectroscopy , microbiology and biotechnology , biology , stereochemistry , enzyme , gene
Expression of recombinant horse heart myoglobin in Escherichia coli has been found to result in the production of both native and variable amounts (~ 16–17% total) of two sulphmyoglobin isomers. The recombinant sulphmyoglobin produced consists primarily of the A and B isomers as identified by 1 H NMR spectroscopy with no evidence for production of the C isomer. Conversion of recombinant sulphmyoglobin to the native protein can be achieved by reconstitution with protohaem IX. The possible relationship of this observation to recombinant expression of other heme proteins is discussed.