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• W1973414985 abstract "We isolated cDNA clones for cytochromes b561 from sheep and porcine adrenal medullae using the RT-PCR technique. Comparison of the deduced amino acid sequences of various species showed that there are two fully-conserved regions in this cytochrome. In addition, one methionyl and six histidyl residues (potential heme ligands) are fully-conserved. Based on a plausible structural model in which a polypeptide spans the vesicle membranes six times and holds two heme B molecules, the first conserved sequence (69ALLVYRVFR77) is located on the extravesicular side of an α-helical segment and the second one (120SLHSW124) is located in an intravesicular loop connecting two α-helical segments, respectively. Consideration of the relative locations of the fully-conserved sequences, and the methionyl and histidyl residues in the model led to a proposal that the first and second conserved sequences are likely to form the binding sites for extravesicular ascorbic acid and intravesicular semidehydroascorbic acid, respectively. A mild alkaline-treatment of purified bovine cytochrome b561 in oxidized state led to a specific loss of an electron-accepting ability from ascorbic acid for a half of the heme center, suggesting a distinct role for each of the two hemes." @default.
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• W1973414985 date "1998-04-01" @default.
• W1973414985 modified "2023-10-11" @default.
• W1973414985 title "Structural basis for the electron transfer across the chromaffin vesicle membranes catalyzed by cytochrome b561: analyses of cDNA nucleotide sequences and visible absorption spectra" @default.
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• W1973414985 doi "https://doi.org/10.1016/s0167-4838(97)00216-1" @default.
• W1973414985 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9602148" @default.
• W1973414985 hasPublicationYear "1998" @default.
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