Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange.

Abstract

Multidimensional NMR methods were used to obtain 1H-15N correlations and 15N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe2S2 ferredoxin, which acts as the physiological reductant of cytochrome P-450cam (CYP101). A model for the solution structure of oxidized Pdx has been determined recently… (More)

Topics

Cite this paper

@article{Lyons1996RedoxdependentDO, title={Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange.}, author={Terry Lyons and G. Ratnaswamy and Thomas C Pochapsky}, journal={Protein science : a publication of the Protein Society}, year={1996}, volume={5 4}, pages={627-39} }