Metabolism, Structure and Function of Plant Tetrapyrroles: Volume 90

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Metabolism, Structure and Function of Plant Tetrapyrroles: Volume 90 Editor: Bernhard Grimm Format: Hardback First Published: Published By: Elsevier Science & Technology
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Pages: 328 Language: English ISBN: 9780081027523 Categories: , , , ,

Metabolism, Structure and Function of Plant Tetrapyrroles, Volume 90, the latest release in the Advances in Botanical Research series is a compilation of the current state-of-the-art on the topic. Chapters in this new release cover Tetrapyrrole Pigments of Photosynthetic Antennae and Reaction Centers of Higher Plants: Biochemistry, Biophysics, Functions, Molecular Mechanism of Antenna Regulation, Applications, Chlorophyll c: Synthesis, Occurrence, Light-Harvesting, Absorbance, Excitation Properties, Pigment Organization in Chlorophyll-Binding Proteins (FCP), Chlorophyll d and f: Synthesis, Occurrence, Light-harvesting, Absorbance, Excitation Properties, Pigment Organization in Chlorophyll-Binding Protein Complexes, Analysis of Chlorophyll, Precursors and Derivatives by New High-Performance Liquid Chromatography and Mass Spectrometry, and much more.

Weight0.64 kg
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Author Biography

Bernhard Grimm is Professor of Plant Physiology at the Institute of Biology at the Humboldt-Universität zu Berlin and Dean of the Faculty of Life Science. He studied biology at the University of Hannover and performed doctoral studies in the group of Prof. Klaus Kloppstech. He spent five years at a postdoctoral fellow and research assistant in the Department of Prof. Diter von Wettstein at the Carlsberg Laboratory, before he moved as group leader to the Institute of Plant Genetics and Crop Plant Research (IPK) in Gatersleben, Germany. Finally, he was appointed at the Humboldt University in January 2001. His current research interests cover several aspects of photosynthesis and chloroplast biogenesis: tetrapyrrole biosynthesis, plastid-derived retrograde signalling, riboflavin biosynthesis, the assembly of chlorophyll-binding proteins, posttranslational and cotranslational mechanisms in chloroplasts.