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A Structural Basis of Light Energy and Electron Transfer in Biology (Nobel Lecture)†‡
Prof. Dr. Robert Huber,
Corresponding Author
Prof. Dr. Robert Huber
Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033 Martinsried (FRG)
Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033 Martinsried (FRG)Search for more papers by this authorProf. Dr. Robert Huber,
Corresponding Author
Prof. Dr. Robert Huber
Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033 Martinsried (FRG)
Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033 Martinsried (FRG)Search for more papers by this author†
Copyright © The Nobel Foundation 1989.—We thank the Nobel Foundation, Stockholm for permission to print this lecture.
‡
Dedicated to Christa
Abstract
Aspects of intramolecular light energy and electron transfer are discussed for three protein cofactor complexes whose three-dimensional structures have been elucidated by X-ray crystallography: the light harvesting phycobilisomes of cyanobacteria, the reaction center of purple bacteria, and the blue multi-copper oxidases. A wealth of functional data is available for these systems which allows specific correlations to be made between structure and function and general conclusions to be drawn about light energy and electron transfer in biological materials.
Abstract
Solar energy and its role as the energetic basis of terrestial life continue to attract interest now as ever – and not only in connection with oil crises and the ozone hole! How are light energy and electrons transferred in Nature? Which chemical compounds are required for this purpose? What relationships exist between structure and function? Does the photosynthetic reaction center of bacteria correspond to that of plants? Answers to these and further questions have been found by Robert Huber, Johann Deisenhofer and Hartmut Michel through the extremely meticulous crystallization and X-ray structure analysis of pigment protein systems, for which the three authors were awarded the 1988 Nobel Prize in Chemistry.
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