Ferric His93Gly myoglobin cavity mutant and its complexes with thioether and selenolate as heme protein models
作者： Jing Du , Masanori Sono , John H. Dawson
DOI: 10.1142/S1088424610002872
关键词:
摘要: The composition of ferric exogenous ligand-free His93Gly sperm whale myoglobin (H93G Mb) at neutral pH has been determined by examination the spectral properties protein over range from 3.0 to 10.5. An apparent pKa value ~6.6 observed for conversion a postulated six-coordinate bis-water-bound coordination structure 5.0 five-coordinate hydroxide-bound form Starting H93G protein, mono- and bis-thioether (tetrahydrothiophene, THT)-ligated adducts have prepared characterized UV-visible (UV-vis) absorption magnetic circular dichroism (MCD) spectroscopy. mon-THT Mb species hydroxide as sixth ligand. bis-THT derivative is model low-spin heme binding site native bis-Met-ligated bacterioferritin or streptococcal heme-associated (Shp). A novel THT-bound ferryl moiety partially formed. high-spin H93G(selenolate) complex using benzeneselenol UV-vis MCD spectroscopy Se-Cys-ligated cytochrome P450. results described herein further demonstrate versatility cavity mutant modeling structures iron active sites.
sci-hub.se 参考文章(41)
Eraldo Antonini, Maurizio Brunori, Hemoglobin and myoglobin in their reactions with ligands ,(1971)
Deborah S. Wuttke, Harry B. Gray, Protein engineering as a tool for understanding electron transfer Current Opinion in Structural Biology. ,vol. 3, pp. 555- 563 ,(1993) , 10.1016/0959-440X(93)90083-W
Roman Aranda, Chad E. Worley, Mengyao Liu, Eduard Bitto, M. Susan Cates, John S. Olson, Benfang Lei, George N. Phillips, Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp. Journal of Molecular Biology. ,vol. 374, pp. 374- 383 ,(2007) , 10.1016/J.JMB.2007.08.058
T.L. Poulos, Ligands and electrons and haem proteins Nature Structural & Molecular Biology. ,vol. 3, pp. 401- 403 ,(1996) , 10.1038/NSB0596-401
Gia D. DePillis, Sean M. Decatur, Doug Barrick, Steven G. Boxer, FUNCTIONAL CAVITIES IN PROTEINS : A GENERAL METHOD FOR PROXIMAL LIGAND SUBSTITUTION IN MYOGLOBIN Journal of the American Chemical Society. ,vol. 116, pp. 6981- 6982 ,(1994) , 10.1021/JA00094A081
Mark P Roach, Waheeda J Puspita, Yoshihito Watanabe*, Proximal ligand control of heme iron coordination structure and reactivity with hydrogen peroxide: investigations of the myoglobin cavity mutant H93G with unnatural oxygen donor proximal ligands. Journal of Inorganic Biochemistry. ,vol. 81, pp. 173- 182 ,(2000) , 10.1016/S0162-0134(00)00101-X
Masanori Sono, Mark P. Roach, Eric D. Coulter, John H. Dawson, Heme-Containing Oxygenases Chemical Reviews. ,vol. 96, pp. 2841- 2888 ,(1996) , 10.1021/CR9500500
Mark P. Roach, Alycen E. Pond, Melissa R. Thomas, Steven G. Boxer, John H. Dawson, The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems: Thiolate Adducts of the Myoglobin H93G Cavity Mutant Journal of the American Chemical Society. ,vol. 121, pp. 12088- 12093 ,(1999) , 10.1021/JA9915504
Paul D. Barker, Edmund P. Nerou, Myles R. Cheesman, Andrew J. Thomson, Pedro de Oliveira, H. Allen O. Hill, Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties. Biochemistry. ,vol. 35, pp. 13618- 13626 ,(1996) , 10.1021/BI961127X
Raymond F. Burk, Kristina E. Hill, Selenoprotein P-expression, functions, and roles in mammals. Biochimica et Biophysica Acta. ,vol. 1790, pp. 1441- 1447 ,(2009) , 10.1016/J.BBAGEN.2009.03.026