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th  - 1987 - 51st ENC Conference

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WF2<br />

LrIII~ITY OF NUC].FAR OVERHAUSER EXPERIMENTS IN THE S'IXJDY OF<br />

]-IEME PROTEINS<br />

V. Thanabal, W. S. Smi<strong>th</strong>, M. J. Chatfield, S. D. Emerson,<br />

J. L. McGourty, J. Hauksson, D. H. Peyton, J. T. J. Lecomte,<br />

K.-B. Lee, and G. N. La Mar*<br />

Dept. of Chemistry, University of California, Davis, CA 95616<br />

The paramagnetic center of heme proteins also contributes<br />

significantly to relaxation such <strong>th</strong>at it becomes very difficult to<br />

saturate resonances which arise from protons near <strong>th</strong>e iron wi<strong>th</strong>out<br />

significantly perturbing <strong>th</strong>e rest of <strong>th</strong>e spectrum via off-resonance<br />

effects. In addition, <strong>th</strong>e systems have high molecular weights,<br />

leading to <strong>th</strong>e usual spin-diffusion effects.<br />

We have developed me<strong>th</strong>ods of using <strong>th</strong>e nuclear Overhauser<br />

effect in paramagnetic hemoproteins in <strong>th</strong>e light of <strong>th</strong>e problems<br />

mentioned above. Included in <strong>th</strong>is study are numerical solutions of<br />

<strong>th</strong>e Bloch equations evaluating <strong>th</strong>e off-resonance effects expected<br />

when using high saturating power on a system of fast-relaxing<br />

protons. Fur<strong>th</strong>er, we provide examples of uses we have found for<br />

nuclear Overhauser effect studies in paramagnetic heine proteins<br />

wi<strong>th</strong> molecular weights ranging up to greater <strong>th</strong>an 75,000.

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