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• W1978321844 abstract "In c-type cytochromes, heme is attached to the polypeptide via thioether linkages between vinyl groups on the tetrapyrrole ring and cysteine thiols in a CX(2)CH motif. To study the role of the heme-binding site in c-type cytochrome assembly and function, we generated amino acid changes in this region of Rhodobacter sphaeroides cytochrome c(2) ((15)Cys-Gln-Thr-Cys-His(19)). Amino acid substitutions at Cys(15), Cys(18), or His(19) produced mutant proteins that did not support growth via photosynthesis where this electron carrier is required. Many of these changes appeared to slow signal peptide removal, suggesting that heme attachment is coupled to processing of the c-type cytochrome precursor protein. Inserting an alanine between the cysteine ligands (CycA-Ins17A) did not significantly alter the behavior of this protein in vivo and in vitro, suggesting that the existence of 2 residues between cysteine thiols is not essential for heme attachment to a Class I c-type cytochrome like cytochrome c(2)." @default.
• W1978321844 created "2016-06-24" @default.
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• W1978321844 date "2001-05-01" @default.
• W1978321844 modified "2023-09-23" @default.
• W1978321844 title "Characterization of Rhodobacter sphaeroides Cytochrome c2 Proteins with Altered Heme Attachment Sites" @default.
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• W1978321844 doi "https://doi.org/10.1006/abbi.2001.2330" @default.
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