| Citation | Distinguished for his innovative applications of NMR spectroscopy in organic and biological chemistry, for his biomimetic porphyrin systems, and his theory of pi-pi interactions. His early explorations of lanthanide shift reagents greatly enhanced the power of NMR to solve questions of structure and conformation for the organic chemist. He then pioneered the use of NOE difference spectroscopy in organic chemistry, his achievements including the first complete analyses of the proton spectra of steroids. Sanders' techniques for acquiring, manipulating and interpreting NOE difference spectra have become world-wide standard laboratory practice. His notable contributions to biological chemistry through NMR include the first measurement of an enzymic kinetic isotope effect in live cells, and the use of deuterium NMR to elucidate the substrate specificity and absolute stereochemistry of intracellular bacterial formaldehyde dismutases. Most importantly, he has resolved many of the long-standing paradoxes between the known in situ enzymology and the apparently contradictory physical chemistry of isolated granules. Sanders is responsible for the creation and study of numerous model photosynthetic and enzymic systems based on porphyrins. These studies gave one of the first experimental verifications of the long-sought Marcus 'inverted region' in photoinduced electron transfer, and led to the development of a general model explaining pi-pi interactions. The model for pi-pi interactions, and its derived geometrical rules, is relevant to the structure of DNA duplexes and proteins; it promises to make a major impact in many areas. Like much of Sanders' work, it demolishes well-entrenched preconceptions through the clear use of simple insights and the deliberate crossing of disciplinary boundaries. |