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Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXAStructure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA
Structural highlights
FunctionPEBS_BPPRM Plays a role in phycoerythrobilin biosynthesis, the red pigment chromophore photosynthetically active biliproteins of the host cyanobacteria. Uses a four-electron reduction to carry out the reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host. Publication Abstract from PubMedPhycoerythrobilin (PEB) is a pink-colored open-chain tetrapyrrole molecule found in the cyanobacterial light-harvesting phycobilisome. Within the phycobilisome, PEB is covalently bound via thioether bonds to conserved cysteine residues of the phycobiliprotein subunits. In cyanobacteria, biosynthesis of PEB proceeds via two subsequent two-electron reductions catalyzed by the ferredoxin-dependent bilin reductases (FDBR) PebA and PebB starting from the open-chain tetrapyrrole biliverdin IXalpha. Recently, a new member of the FDBR family was identified in the genome of a marine cyanophage. In contrast to the cyanobacterial enzymes, PEB-synthase (PebS) from cyanophage combines both two-electron reductions for PEB synthesis. Here we show that PebS acts via a substrate radical mechanism and that two conserved aspartate residues at position 105 and 206 are critical for stereospecific substrate protonation and conversion. Based on the crystal structures of both PebS variants and presented biochemical and biophysical data a mechanism for BV conversion to PEB is postulated and discussed with respect to other FDBR family members. Radical mechanism of cyanophage phycoerythrobilin synthase (PebS).,Busch AW, Reijerse EJ, Lubitz W, Hofmann E, Frankenberg-Dinkel N Biochem J. 2010 Nov 4. PMID:21050180[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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