title: On the structure and function of cytochrome b-559.
abstract: A sumary of biochemical, biophysical, and molecular biological data is presented which led to the identification of two different polypeptides (α and β, MW=9.16 and 4.27 kDa) in the cytochrome b-559 protein. The presence of a single His residue on each polypeptide, and the conclusion from spectroscopy that the heme coordination must be bis-histidine led to an obligatory requirement for coordination of a single heme through a heme cross-linked dimer. This structure does not have a precedent among soluble or membrane bound cytochromes. The possible participation of the cytochrome in the pathway of photoactivation is discussed.
authors.affiliation: Department of Biological Sciences Lilly Hall of Life Sciences, Purdue University, 47907, West Lafayette, Indiana, (U.S.A.).
authors.forename: W A
authors.initials: WA
authors.lastname: Cramer
authors.forename: S M
authors.initials: SM
authors.lastname: Theg
authors.forename: W R
authors.initials: WR
authors.lastname: Widger