Premium
A model for the molecular organization of cytochrome β‐561 in chromaffin granule membranes
Author(s) -
Esposti M.Degli,
Kamensky Yu.A.,
Arutjunjan A.M.,
Konstantinov A.A.
Publication year - 1989
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(89)81012-9
Subject(s) - hemeprotein , chemistry , membrane , granule (geology) , heme , cytochrome c , cytochrome , biophysics , biochemistry , transmembrane protein , mitochondrion , biology , enzyme , paleontology , receptor
The CD spectrum of reduced cytochrome (cyt.) β‐561 in chromaffin granule membranes resembles that of mitochondrial cyt. β 1 and indicates possible heme‐heme interaction in the protein. Based on spectroscopic data and analysis of the amino acid sequence, a model of cyt. β‐561 is suggested, in which the protein carries two transmembrane‐localized hemes, each coordinated by two histidines. The model accounts for the presence of two different forms of cyt. β‐561 in chromaffin granule membranes and provides a mechanism of transmembrane electron transfer by this hemoprotein.