Prediction and comparison of the haem-binding sites in membrane haemoproteins.
This article contains a comparative review of the structural properties of membrane haemoproteins, with particular emphasis on the possible similarities of the haem-binding peptides. A procedure is suggested for identifying the peptides which may bind membrane-buried haems on the basis of the primary sequences of the proteins. The integration of this procedure with the information deduced by refined hydropathy analysis indicates that the basic structural model for the haemoproteins which interact with quinones may be a transmembrane helical bundle containing the haem(s) at its centre. Structural similarities exist in the sequence of hydrophobic segments that are predicted to bind the membrane-buried haems of b-cytochromes which interact with quinones. The predicted haem-binding sites show similarities also with the peptides that bind the non-haem iron in the bacterial reaction centres, and this may be correlated to the common function of interacting with quinones and their intermediates. The analysis of the amino-acid composition of the proposed ligand peptides in the membrane haemoproteins examined has provided a molecular rationale for explaining the highly anisotropic low-spin EPR signal which is characteristic of many membrane-bound b-cytochromes.
Esposti
M D
MD
Department of Biology, University of Bologna, Italy.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D003573:Cytochrome b Group / Q000378:metabolism; D006418:Heme / Q000378:metabolism*; D006420:Hemeproteins / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D011809:Quinones / Q000378:metabolism
D003573:Cytochrome b Group; D006420:Hemeproteins; D008565:Membrane Proteins; D011809:Quinones; D006418:Heme; D006639:Histidine