Determining Rieske cluster reduction potentials

被引:37
作者
Brown, Eric N. [1 ]
Friemann, Rosmarie [2 ]
Karlsson, Andreas [2 ]
Parales, Juan V. [3 ]
Couture, Manon M. -J. [4 ]
Eltis, Lindsay D. [5 ]
Ramaswamy, S. [1 ]
机构
[1] Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA
[2] Swedish Univ Agr Sci, Ctr Biomed, Dept Mol Biol, Uppsala, Sweden
[3] Univ Calif Davis, Microbiol Sect, Davis, CA 95616 USA
[4] Medicago R&D, Ste Foy, PQ G1V 3V9, Canada
[5] Univ British Columbia, Dept Microbiol & Immunol, Vancouver, BC V6T 1Z3, Canada
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2008年 / 13卷 / 08期
关键词
Electrochemistry; X-ray crystallography; Rieske ferredoxin;
D O I
10.1007/s00775-008-0413-4
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
The Rieske iron-sulfur proteins have reduction potentials ranging from -150 to +400 mV. This enormous range of potentials was first proposed to be due to differing solvent exposure or even protein structure. However, the increasing number of available crystal structures for Rieske iron-sulfur proteins has shown this not to be the case. Colbert and colleagues proposed in 2000 that differences in the electrostatic environment, and not structural differences, of a Rieske proteins are responsible for the wide range of reduction potentials observed. Using computational simulation methods and the newly determined structure of Pseudomonas sp. NCIB 9816-4 naphthalene dioxygenase Rieske ferredoxin (NDO-F9816-4), we have developed a model to predict the reduction potential of Rieske proteins given only their crystal structure. The reduction potential of NDO-F9816-4, determined using a highly oriented pyrolytic graphite electrode, was - 150 +/- 2 mV versus the standard hydrogen electrode. The predicted reduction potentials correlate well with experimentally determined potentials. Given this model, the effect of protein mutations can be evaluated. Our results suggest that the reduction potential of new proteins can be estimated with good confidence from 3D structures of proteins. The structure of NDO-F9816-4 is the most basic Rieske ferredoxin structure determined to date. Thus, the contributions of additional structural motifs and their effects on reduction potential can be compared with respect to this base structure.
引用
收藏
页码:1301 / 1313
页数:13
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