ELECTRON SELF-EXCHANGE IN HIGH-POTENTIAL IRON-SULFUR PROTEINS - CHARACTERIZATION OF PROTEIN-I FROM ECTOTHIORHODOSPIRA-VACUOLATA

被引:42
作者
BERTINI, I
GAUDEMER, A
LUCHINAT, C
PICCIOLI, M
机构
[1] UNIV PARIS 11,INST CHIM MOLEC,F-91405 ORSAY,FRANCE
[2] UNIV BOLOGNA,INST AGR CHEM,I-40126 BOLOGNA,ITALY
关键词
D O I
10.1021/bi00210a042
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
During previous research on oxidized and reduced high-potential iron-sulfur proteins (HiPIP hereafter), qualitative different electron self-exchange rates were noticed. We have now investigated this phenomenon in detail for HiPIP I and II from Ectothiorhodospira vacuolata, which differ significantly in total charge and in which the sequence homology is the largest among all known HiPIPs. We have also characterized the electronic structure of HiPIP I through H-1 NMR and EPR spectroscopies to parallel the existing characterization of HiPIP II and other HiPIPs. This investigation has allowed us to propose a model, according to which the productive collisions for electron transfer occur through a hydrophobic patch near the cluster. The effects of total charge and redox potential are considered. The possible formation of dimers through the hydrophobic patch at liquid helium temperature is discussed in light of the EPR spectra.
引用
收藏
页码:12887 / 12893
页数:7
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