In contrast to Lba2+, Lbam2+ showed aberrant spectra when bound with either O2 or CO.
Lbam2+ also bound nicotinate and showed absorption spectra indistinguishable from those of Lba2+ nicotinate. The 3 Lbam fractions were reduced by dithionite or by NADH in the presence of riboflavin. Upon binding with nicotinate, the alpha and beta bands were shifted significantly into the red region compared with the Lba3+ nicotinate complex. These modified pigments showed a hypochromic shift of 10 nm for the charge transfer absorption maximum however, differences were not apparent in the Soret region. The ferric forms of these pigments were green and showed anomalous spectra in the visible region compared with the Lba3+ forms.
Three modified haemoprotein derivatives of the leghaemoglobin Lba (Lbam1, Lbam2 and Lbam3) were purified by preparative isoelectric focusing from root nodules of 40- to 50-d-old soyabean cv.
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