Conformational stability of ferricytochrome c near the heme in its complexwith heparin in alkaline pH

The stability of the methionine 80 sulfur-heme iron bond of ferricytochrome c (cyt c) in its complex with heparin has been studied by absorption spect roscopy in the alkaline pH region at temperatures of 20-80 degreesC and low ionic strength. According to spectral data, the midtransition temperature (T-1/2) of the cleavage of the sulfur-iron bond was 57.5 +/- 0.5 and 52.5 /- 0.5 degreesC for cytochrome c and cytochrome c-heparin complex, respecti vely, at neutral pH. The increasing in pH caused an expressive fall of cyt c transition temperature while the T-1/2 for cyt c in its complex with hepa rin was constant and from pH > 7.7, this value was higher than that for the free cyt c. Addition of heparin to cyt c evoked a moderate increase of 695 nm band intensity at neutral or slightly alkaline pH. It was shown that he parin stabilises the conformation or cyt c in state III (the Met 80-heme ir on bond is presented) in alkaline pH region and physiological temperature r ange. (C) 2001 Elsevier Science Ltd. All rights reserved.