Sandbox Reserved 1501: Difference between revisions
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<!-- Global Stoichiometry Homotetramer A4 --> | <!-- Global Stoichiometry Homotetramer A4 --> | ||
Flavocytochrome b(2) is a tetrameric enzyme (Jacq and Lederer, 1972 and 1974<ref> | Flavocytochrome b(2) is a tetrameric enzyme (Jacq and Lederer, 1972 and 1974<ref>PMID: 4336855</ref>,<ref>PMID: 4152980</ref>). Each of the four identical subunits is composed by one single polypeptide chain. | ||
Each subunit contains a binding site for the selectively non-covalently binding of the cofactor FMN(3-) (Flavinmononucleotide), as well as one in with the iron complexed in the tetrapyrrole ring interacts with heme b(2-) cofactor (Risler and Groudinsky, 1973<ref>PMID: 5545004 </ref>). | Each subunit contains a binding site for the selectively non-covalently binding of the cofactor FMN(3-) (Flavinmononucleotide), as well as one in with the iron complexed in the tetrapyrrole ring interacts with heme b(2-) cofactor (Risler and Groudinsky, 1973<ref>PMID: 5545004 </ref>). | ||
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<!-- https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60344--> | <!-- https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60344--> | ||
The amino acid sequence in the heme binding region was first determined by Guidard ''et al'', 1974<ref> | The amino acid sequence in the heme binding region was first determined by Guidard ''et al'', 1974<ref>PMID: 4575975</ref>. | ||
For every subunit of the wild type protein form, the crystallized preparation analysis determined a molecular weight of the chain of 36 kD (Appleby and Morton, 1959<ref>PMID: 13638255</ref>) and the chain of 21 kD (Jacq and Lederer, 1974<ref>PMID: 4152980</ref>). | For every subunit of the wild type protein form, the crystallized preparation analysis determined a molecular weight of the chain of 36 kD (Appleby and Morton, 1959<ref>PMID: 13638255</ref>) and the chain of 21 kD (Jacq and Lederer, 1974<ref>PMID: 4152980</ref>). | ||
The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref>PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein. | The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref>PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein. | ||
