Literature summary for 1.3.7.5 extracted from

Stoll, S.; Gunn, A.; Brynda, M.; Sughrue, W.; Kohler, A.C.; Ozarowski, A.; Fisher, A.J.; Lagarias, J.C.; Britt, R.D.
Structure of the biliverdin radical intermediate in phycocyanobilin:ferredoxin oxidoreductase identified by high-field EPR and DFT (2009), J. Am. Chem. Soc., 131, 1986-1995.

Crystallization (Commentary)

Crystallization (Comment)	Organism
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated	Nostoc sp. PCC 7120 = FACHB-418
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated	Synechocystis sp.

Crystallization (Comment)

Organism

high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated

Nostoc sp. PCC 7120 = FACHB-418

high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated

Synechocystis sp.

Protein Variants

Protein Variants	Comment	Organism
D102N	high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated	Nostoc sp. PCC 7120 = FACHB-418
D105N	high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated	Synechocystis sp.
H88Q	the g anisotropy of the biliverdin radical in H88Q is measurably smaller than those of mutant D105N	Synechocystis sp.

Organism

Organism	UniProt	Comment	Textmining
Nostoc sp. PCC 7120 = FACHB-418	Q93TN0	-	-
Synechocystis sp.	Q55891	strain PCC6803	-