Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple scattering analyses of XAFS data

被引:31
作者
Cheng, MC [1 ]
Rich, AM [1 ]
Armstrong, RS [1 ]
Ellis, PJ [1 ]
Lay, PA [1 ]
机构
[1] Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia
关键词
D O I
10.1021/ic990395r
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
X-ray absorption fine structure (XAFS) data were obtained from frozen aqueous solutions (10 K) of horse heart ferri- and ferrocyt c. Models of the structure about the Fe center were refined to optimize the fit between the observed XAFS in the range 0 less than or equal to k less than or equal to 16.3 Angstrom(-1) and the XAFS calculated using both single-scattering (SS) and multiple-scattering (MS) calculations. The bond lengths obtained are more accurate and precise than those determined previously for cyt c from various species using X-ray crystallography. The Fe-N bond lengths are 1.98-1.99 Angstrom for both oxidation states of cyt c. The Fe-S bond of ferricyt c (2.33 Angstrom) is significantly longer than that of ferrocyt c (2.29 Angstrom). The small changes in the bond lengths are consistent with the small reorganizational energy required for the fast electron-transfer reaction of cyt c.
引用
收藏
页码:5703 / 5708
页数:6
相关论文
共 38 条
[31]   Determination of the Fe-ligand bond lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using multiple-scattering XAFS analyses [J].
Rich, AM ;
Armstrong, RS ;
Ellis, PJ ;
Lay, PA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (42) :10827-10836
[32]  
RICH AM, 1997, THESIS U SYDNEY
[33]  
Scheidt W.R., 1987, J STRUCT BONDING BER, V64, P1, DOI DOI 10.1007/BFB0036789
[34]   X-RAY ABSORPTION SPECTROSCOPY OF BIOLOGICAL MOLECULES [J].
SHULMAN, RG ;
EISENBERGER, P ;
KINCAID, BM .
ANNUAL REVIEW OF BIOPHYSICS AND BIOENGINEERING, 1978, 7 :559-578
[35]   CONFORMATION CHANGE OF CYTOCHROME-C .1. FERROCYTOCHROME-C STRUCTURE REFINED AT 1.5 A RESOLUTION [J].
TAKANO, T ;
DICKERSON, RE .
JOURNAL OF MOLECULAR BIOLOGY, 1981, 153 (01) :79-94
[36]   Effects of ligation and folding on reduction potentials of heme proteins [J].
Tezcan, FA ;
Winkler, JR ;
Gray, HB .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (51) :13383-13388
[37]   A multiplet analysis of Fe K-edge 1s->3d pre-edge features of iron complexes [J].
Westre, TE ;
Kennepohl, P ;
DeWitt, JG ;
Hedman, B ;
Hodgson, KO ;
Solomon, EI .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (27) :6297-6314
[38]   SPECTROSCOPIC AND THEORETICAL DESCRIPTION OF THE ELECTRONIC-STRUCTURE OF THE S = 3/2 NITROSYL COMPLEX OF NONHEME IRON ENZYMES [J].
ZHANG, Y ;
PAVLOSKY, MA ;
BROWN, CA ;
WESTRE, TE ;
HEDMAN, B ;
HODGSON, KO ;
SOLOMON, EI .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1992, 114 (23) :9189-9191