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.
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Cramer, W.A., Theg, S.M. & Widger, W.R. On the structure and function of cytochrome b-559. Photosynth Res 10, 393–403 (1986). https://doi.org/10.1007/BF00118305
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DOI: https://doi.org/10.1007/BF00118305