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Protein Science, Vol 5, Issue 4 627-639, Copyright © 1996 by Cold Spring Harbor Laboratory Press

ARTICLE

Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange

T. A. LYONS, G. RATNASWAMY and T. C. POCHAPSKY
Department of Biology, Brandeis University, Waltham, Massachusetts 02254-9110

Multidimensional NMR methods were used to obtain (1)H-(15)N correlations and (15)N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe(2)S(2) ferredoxin, which acts as the physiological reductant of cytochrome P-450(cam) (CYP101). A model for the solution structure of oxidized Pdx has been determined recently using NMR methods (Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, 1994, Biochemistry 33:6424-6432) and redox-dependent (1)H NMR spectral features have been described (Pochapsky TC, Ratnaswamy G, Patera A, 1994, Biochemistry 33:6433-6441). (15)N assignments were made with NOESY-((1)H/(15)N) HMQC and TOCSY-((1)H/(15)N) HSQC spectra obtained using samples of Pdx uniformly labeled with (15)N. Local dynamics in both oxidation states of Pdx were then characterized by comparison of residue-specific amide proton exchange rates, which were measured by a combination of saturation transfer and H(2)O/D(2)O exchange methods at pH 6.4 and 7.4 (uncorrected for isotope effects). In general, where exchange rates for a given site exhibit significant oxidation-state dependence, the oxidized protein exchanges more rapidly than the reduced protein. The largest dependence of exchange rate upon oxidation state is found for residues near the metal center and in a region of compact structure that includes the loop-turn Val 74-Ser 82 and the C-terminal residues (Pro 102-Trp 106). The significance of these findings is discussed in light of the considerable dependence of the binding interaction between Pdx and CYP101 upon the oxidation state of Pdx.
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