Polytungstate binding to metmyoglobin: an access to various structural forms of the protein.
Complex formation between metMb and three heteropolytungstates, offering various sizes and charges, has been studied in the pH range 6-8. 1:1 complexes are formed with (KAs4W40O140)27- and (NaSb9W21O86)18-, with an association constant of 10(6) and 4 x 10(5) M-1 respectively, at pH 7.3 and 10 mM ionic strength. Resulting structural changes of the metMb moiety have been investigated by absorption, CD and EPR spectroscopies. Besides an acid-denatured-like form, obtained at a pH as high as 6.5 with the largest polyanion, the formation of an hemichrome is generally observed. It can be reduced to the hemochrome, whereas the complexation of deoxyMb by the polytungstates leaves the deoxy structure unaltered.
Chottard
G
G
Laboratoire de Physicochimie Inorganique URA 419, Universite Pierre et Marie Curie, Paris, France.
el Ajouz
N
N
Herve
G
G
D000965:Antimony; D001151:Arsenic; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D008786:Metmyoglobin / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012825:Silicon; D013053:Spectrophotometry; D014414:Tungsten / Q000378:metabolism*; D017973:Tungsten Compounds
D017973:Tungsten Compounds; D008786:Metmyoglobin; D000965:Antimony; D001151:Arsenic; C045951:tungstate; D014414:Tungsten; D012825:Silicon