MAGNETIC RELAXATION STUDIES OF COORDINATED SOLVENT MOLECULES IN METALLOPROTEINS

• 作 者: SeymourH.Koenig RodneyD.Brown Ⅲ
• 机 构: IBM Thomas J.Watson Research Center Yorktown Heights,New York 10598,IBM Thomas J.Watson Research Cen
• 出 处: 分子科学与化学研究
• 发表日期: 1982年04期
• 关键词: relaxation quids analogous inadequate readily paramagnetic complexes advent inte

IN the early investigations of nuclear magnetic resonance in li-quids,paramagnetic ions were added to regulate the magnetic re-laxation rates of solvent protons and to study the ion-solventcomplexes formed.The theory of relaxation that was developedas experimental techniques improved was very successful for de-scribing the observed relaxation.However,the same theory ap-plied to analogous studies of solutions in which these paramagne-tic ions are complexed with protein gave ambiguous results.Withthe advent of NMRD data (i.e.,relaxation rate as a function ofmagnetic field),it became increasingly clear that the theoryadequate for aquoions was inadequate for ion-protein complexes.We trace this history,in part using data now readily attainablewith greatly improved instrumentation,and show that the majorreason for the inadequacy relates to the need for new models forsolvent-protein interactions.The phenomena are far richer thanoriginally anticipated.