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  • Influence
A Red-Shifted Chlorophyll
TLDR
It is proposed that chlorophyll f is [2-formyl]-chlorophyll a (C55H70O6N4Mg), which suggests that oxygenic photosynthesis can be extended further into the infrared region and may open associated bioenergy applications. Expand
Biliprotein maturation: the chromophore attachment
TLDR
Methodological advances in the process, as well as the finding of often large numbers of homologues, opens new possibilities for research on the subsequent assembly/disassembly of the phycobilisome in cyanobacteria and red algae, on the assembly and organization of the cryptophyte light‐harvesting system, on applications in basic research such as protein folding, and on the use of phyCobiliproteins for labelling. Expand
An Overview of Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications
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Structure‐Based Calculations of the Optical Spectra of the LH2 Bacteriochlorophyll‐Protein Complex from Rhodopseudomonas acidophila
Abstract— The molecular structure of the light‐harvesting complex 2 (LH2) bacteriochlorophyll‐protein antenna complex from the purple non‐sulfur photosynthetic bacterium Rhodopseudomonas acidophila,Expand
Chlorophylls and Carotenoids
TLDR
The combination of chlorophylls with carotenoids allows photosynthetic organisms balance between competing for light, and being killed by an overdose. Expand
Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins
  • K. Zhao, P. Su, +7 authors H. Scheer
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences
  • 4 September 2007
TLDR
Using a modular multiplasmidic expression-reconstitution assay in Escherichia coli with low background binding, phycobilin:cystein-84 biliprotein lyase (CpeS1) from Anabaena PCC7120, has been characterized as a nearly universal lyase for the cysteine-84-binding site that is conserved in all biliproteins. Expand
Lyase Activities of CpcS- and CpcT-like Proteins from Nostoc PCC7120 and Sequential Reconstitution of Binding Sites of Phycoerythrocyanin and Phycocyanin β-Subunits*
TLDR
The functions of the encoded proteins were screened in vitro and in a heterologous Escherichia coli system with plasmids conferring biosynthesis of the phycocyanobilin chromophore and of the acceptor proteins β-phycoerythrocyanin (PecB), and no lyase activity was found for the lyase homologues CpcS2 and CpcT2. Expand
The accessory bacteriochlorophyll: a real electron carrier in primary photosynthesis.
  • T. Arlt, S. Schmidt, +4 authors W. Zinth
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 15 December 1993
TLDR
Extensive transient absorbance data are fully consistent with a stepwise electron transfer via the accessory bacteriochlorophyll and an angle between the transition moments of the special pair and the species related with the 0.9-ps kinetic component is found. Expand
Reconstitution of phycobilisome core-membrane linker, LCM, by autocatalytic chromophore binding to ApcE.
TLDR
The lack of homologies with the autocatalytically chromophorylating phytochromes, as well as with the heterodimeric cysteine-alpha84 lyases, indicates that ApcE constitutes a third type of bilin:biliprotein lyase. Expand
Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications
Supplementary material to this book contains the following Adobe-Writer (.pdf) files: an overview of the material, the color coding for the map on the title page), and supporting information forExpand
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