Protein dynamics enhance electronic coupling in electron transfer complexes

被引:33
作者
Chohan, KK
Jones, M
Grossmann, JG
Frerman, FE
Scrutton, NS
Sutcliffe, MJ
机构
[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England
[2] Univ Leicester, Dept Chem, Leicester LE1 7RH, Leics, England
[3] Res Councils Daresbury Lab, Cent Lab, Warrington WA4 4AD, Cheshire, England
[4] Univ Colorado, Sch Med, Dept Pediat, Denver, CO 80262 USA
关键词
D O I
10.1074/jbc.M101341200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Electron-transferring flavoproteins (ETFs) from human and Paracoccus denitrificans have been analyzed by small angle x-ray scattering, showing that neither molecule exists in a rigid conformation in solution. Both ETFs sample a range of conformations corresponding to a large rotation of domain II with respect to domains I and III. A model of the human ETF-medium chain acyl-CoA dehydrogenase complex, consistent with x-ray scattering data, indicates that optimal electron transfer requires domain Il of ETF to rotate by similar to 30 to 50 degrees toward domain I relative to its position in the x-ray structure. Domain motion establishes a new "robust engineering principle" for electron transfer complexes, tolerating multiple configurations of the complex while retaining efficient electron transfer.
引用
收藏
页码:34142 / 34147
页数:6
相关论文
共 44 条
[1]   Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein [J].
Basran, J ;
Chohan, KK ;
Sutcliffe, MJ ;
Scrutton, NS .
BIOCHEMISTRY, 2000, 39 (31) :9188-9200
[2]  
Beinert H., 1963, ENZYMES, P447
[3]   PROTEIN ELECTRON-TRANSFER RATES SET BY THE BRIDGING SECONDARY AND TERTIARY STRUCTURE [J].
BERATAN, DN ;
BETTS, JN ;
ONUCHIC, JN .
SCIENCE, 1991, 252 (5010) :1285-1288
[4]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[5]  
Chohan KK, 1998, PROTEIN PEPTIDE LETT, V5, P231
[6]   The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein [J].
Dwyer, TM ;
Zhang, LN ;
Muller, M ;
Marrugo, F ;
Frerman, F .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1999, 1433 (1-2) :139-152
[7]  
Feigin L., 1987, STRUCTURE ANAL SMALL
[8]   alpha T244M mutation affects the redox, kinetic, and in vitro folding properties of Paracoccus denitrificans electron transfer flavoprotein [J].
Griffin, KJ ;
Dwyer, TM ;
Manning, MC ;
Meyer, JD ;
Carpenter, JF ;
Frerman, FE .
BIOCHEMISTRY, 1997, 36 (14) :4194-4202
[9]   The nature of ligand-induced conformational change in transferrin in solution. An investigation using X-ray scattering, XAFS and site-directed mutants [J].
Grossmann, JG ;
Crawley, JB ;
Strange, RW ;
Patel, KJ ;
Murphy, LM ;
Neu, M ;
Evans, RW ;
Hasnain, SS .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 279 (02) :461-472
[10]   Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module [J].
Gruez, A ;
Pignol, D ;
Zeghouf, M ;
Covès, J ;
Fontecave, M ;
Ferrer, JL ;
Fontecilla-Camps, JC .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (01) :199-212