Type I reversible photochemistry of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore

Zhao, Kai‐Hong; Haeßner, R.; Cmiel, Edmund; Scheer, Hugo

doi:10.1016/0005-2728(94)00181-4

Cited by 57 publications

(96 citation statements)

References 34 publications

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“…Phycoerythrocyanin (PEC) is an integral component of the PBsome antenna in several species of cyanobacteria (Bryant, 1982). Unlike other phycobiliproteins, however, isolated PEC shows a remarkable photochemistry (Bjoern, 1979;Bjoern and Bjoern, 1980;Kufer and Bjoern, 1989;Siebzehnrübl et al, 1989;Zhao and Scheer, 1995). PEC is photoreversibly photochromic, i.e., it undergoes a phototransformation, which is photochemically reversible.…”

Section: Introductionmentioning

confidence: 99%

“…PEC is photoreversibly photochromic, i.e., it undergoes a phototransformation, which is photochemically reversible. This reactivity has been related to the unusual phycoviolobilin-chromophore (PVB) (This chromophore is also referred to as PXB (Bishop et al, 1987)) bound to cys-84 on the α-subunit via a thioether linkage (Füglistaller et al, 1983;Bishop et al, 1987;Zhao et al, 1995). The photochemistry of PEC and its α-subunit (α-PEC) is quite variable.…”

Section: Introductionmentioning

confidence: 99%

“…The photochemistry of PEC and its α-subunit (α-PEC) is quite variable. There are two distinct types of photoreactions, type I (Siebzehnrübl, 1990) and type II Zhao and Scheer, 1995). Recent studies gave increasing evidence for a basic similarity of this type I photochemistry with that of the plant sensory photoreceptor, phytochrome.…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies gave increasing evidence for a basic similarity of this type I photochemistry with that of the plant sensory photoreceptor, phytochrome. Both involve the 15Z/E-isomerization of the bilin chromophore (Zhao et al, 1995), and the optical properties (absorption, fluorescence, circular dichroism) are largely comparable (Maruthi Sai et al, 1993). PEC and other biliproteins have also been implicated in photomorphogenesis of cyanobacteria (Kufer and Bjoern, 1989; Maruthi- Sai et al, 1992, Braune et al, 1988, but direct proof for this is still lacking.…”

Section: Introductionmentioning

confidence: 99%

“…The molecular basis of the photochemistry of α-PEC has been identified as a 15Z/E isomerization of PVB (Zhao et al, 1995). Generally, the initial Z/E isomerization of chromophores in photoreceptors like rhodopsin and phytochrome is followed by series of intermediates (Schaffner et al, 1990;.…”

Section: Introductionmentioning

confidence: 99%

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Intermediates of reversible photochemistry of phycoerythrocyanin α from Mastigocladuslaminosus probed by low temperature absorptionand circular dichroism spectroscopy

Zhao

Scheer²

1999

International Journal of Photoenergy

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Abstract. The reversible photochemistry of the α-subunit of phycoerythrocyanin (α-PEC) has been measured by low temperature absorption and circular dichroism in the range of 125 K to 295 K. Below 185 K, the photochemistry is nearly silent; above 205 K, the photochemistry increases gradually without an indication of intermediates, and between 185 to 205 K spectral changes in absorption and circular dichroism indicate an intermediate and/or changes in the interaction(s) between the chromophore and its environment.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Intermediates of reversible photochemistry of phycoerythrocyanin α from Mastigocladuslaminosus probed by low temperature absorptionand circular dichroism spectroscopy

Zhao

Scheer²

1999

International Journal of Photoenergy

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A Brief History of Phytochromes

2010

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Photosensory proteins enable living things to detect the quantity and quality of their light environment and to transduce that physical signal into biochemical outputs which entrain their metabolism with the ambient light environment. Phytochromes, which photoconvert between red-absorbing Pr and far-red-absorbing Pfr states, have been the most extensively studied of these interesting proteins. Critical regulators of a number of key adaptive processes in higher plants, including photomorphogenesis and shade avoidance, phytochromes are widespread in photosynthetic and nonphotosynthetic bacteria and even in fungi. Cyanobacterial genomes also possess a plethora of more distant relatives of phytochromes known as cyanobacteriochromes (CBCRs). Biochemical characterization of representative CBCRs has demonstrated that this class of photosensors exhibit a broad range of wavelength sensitivities, spanning the entire visible spectrum. Distinct protein-bilin interactions are responsible for this astonishing array of wavelength sensitivities. Despite this spectral diversity, all members of the extended family of phytochrome photosensors appear to share a common photochemical mechanism for light sensing: photoisomerization of the 15/16 double bond of the bilin chromophore.

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Raman Spectra of the Phycoviolobilin Cofactor in Phycoerythrocyanin Calculated by QM/MM Methods

2010

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The Raman spectrum of the phycoviolobilin cofactor of the alpha-subunit of phycoerythrocyanin was computed using a hybrid quantum mechanical/molecular mechanics (QM/MM) method in order to evaluate the performance of the QM/MM approach for calculating the vibrational spectra of protein-bound tetrapyrroles as found in phytochrome photoreceptors. A good overall agreement between the experimental and the calculated spectra was achieved. In addition, calculation of the vibrational properties of several snapshots extracted from a molecular dynamics simulation allowed us to investigate in detail the effect of the protein environment on the vibrational spectra. Heterogeneous broadening of most of the experimental bands could be reproduced in a satisfactory manner as the sum of individual spectra obtained by normal-mode-analysis (NMA). An exception is the bandwidth of the peak at 1646 cm(-1), which is underestimated by the NMA sum as well as by the instantaneous normal mode analysis (INMA) approach.

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Type I reversible photochemistry of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore

Cited by 57 publications

References 34 publications

Intermediates of reversible photochemistry of phycoerythrocyanin α from Mastigocladuslaminosus probed by low temperature absorptionand circular dichroism spectroscopy

Intermediates of reversible photochemistry of phycoerythrocyanin α from Mastigocladuslaminosus probed by low temperature absorptionand circular dichroism spectroscopy

A Brief History of Phytochromes

Raman Spectra of the Phycoviolobilin Cofactor in Phycoerythrocyanin Calculated by QM/MM Methods

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