Stabilization of yeast cytochrome C covalently immobilized on fused silica surfaces.
The surface-enhanced conformational stability of yeast cytochrome c (YCC) covalently immobilized on a fused silica prism with heterobifunctional cross-linkers has been studied by attenuated total reflection absorption spectroscopy using the Soret band of the heme prosthetic group as a probe. Comparison of the results to those of horse cytochrome c physisorbed on the same substrate as well as to the corresponding proteins in solution indicates that the surface plays a significant role in stabilizing the native conformation of the surface-bound YCC. Unfolding to extended configurations was so hindered that the native conformation of the covalently immobilized protein is essentially unaffected by the presence of denaturants such as methanol and 1-propanol.
Cheng
Yo-Yuan
YY
Institute of Atomic and Molecular Sciences, Academia Sinica, P.O. Box 23-116, Taipei, Taiwan 106, R.O.C.
Chang
Huan-Cheng
HC
Hoops
Geoffrey
G
Su
Meng-Chih
MC
D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D045304:Cytochromes c