Effect of solvent viscosity on the heme-pocket dynamics of photolyzed (carbonmonoxy)hemoglobin
作者： E. W. Findsen , J. M. Friedman , M. R. Ondrias
DOI: 10.1021/BI00424A005
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摘要: The heme-pocket dynamics subsequent to carbon monoxide photolysis from human hemoglobin have been monitored as a function of glycerol-water solvent composition with time-resolved resonance Raman spectroscopy. Prompt (geminate) ligand recombination rates and the transient geometry established within 10 ns after appear be largely independent composition. rate relaxation an equilibrium deoxy configuration is, however, quite sensitive These observations suggest that former processes result local, internal motions protein, while proximal heme pocket are predicated upon more global protein dependent viscosity.
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Q H Gibson, J S Olson, R E McKinnie, R J Rohlfs, A kinetic description of ligand binding to sperm whale myoglobin. Journal of Biological Chemistry. ,vol. 261, pp. 10228- 10239 ,(1986) , 10.1016/S0021-9258(18)67514-3
S.D. Carson, C.A. Wells, E.W. Findsen, J.M. Friedman, M.R. Ondrias, Interspecies variations in the transient heme species generated subsequent to CO photolysis from hemoglobins. Journal of Biological Chemistry. ,vol. 262, pp. 3044- 3051 ,(1987) , 10.1016/S0021-9258(18)61466-8
J M Friedman, T W Scott, R A Stepnoski, M Ikeda-Saito, T Yonetani, The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study. Journal of Biological Chemistry. ,vol. 258, pp. 10564- 10572 ,(1983) , 10.1016/S0021-9258(17)44493-0
B F Campbell, D Magde, V S Sharma, Geminate recombination of CO in rabbit, opossum, and adult hemoglobins. Journal of Biological Chemistry. ,vol. 260, pp. 2752- 2756 ,(1985) , 10.1016/S0021-9258(18)89425-X
J. Terner, J. D. Stong, T. G. Spiro, M. Nagumo, M. Nicol, M. A. El-Sayed, Picosecond resonance Raman spectroscopic evidence for excited-state spin conversion in carbonmonoxy-hemoglobin photolysis. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 78, pp. 1313- 1317 ,(1981) , 10.1073/PNAS.78.3.1313
Arthur M. Lesk, Cyrus Chothia, Mechanisms of domain closure in proteins Journal of Molecular Biology. ,vol. 174, pp. 175- 191 ,(1984) , 10.1016/0022-2836(84)90371-1
J. Friedman, Structure, dynamics, and reactivity in hemoglobin Science. ,vol. 228, pp. 1273- 1280 ,(1985) , 10.1126/SCIENCE.4001941
Brian B. Hasinoff, S. Bano Chishti, Viscosity dependence of the kinetics of the diffusion-controlled reaction of carbon monoxide with the separated .alpha. and .beta. chains of hemoglobin Biochemistry. ,vol. 22, pp. 58- 61 ,(1983) , 10.1021/BI00270A008
Thomas W. Scott, Joel M. Friedman, Tertiary-structure relaxation in hemoglobin: a transient Raman study Journal of the American Chemical Society. ,vol. 106, pp. 5677- 5687 ,(1984) , 10.1021/JA00331A044
J. L. Martin, A. Migus, C. Poyart, Y. Lecarpentier, R. Astier, A. Antonetti, Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant Proceedings of the National Academy of Sciences of the United States of America. ,vol. 80, pp. 173- 177 ,(1983) , 10.1073/PNAS.80.1.173