60
V. K. Kannaujiya et al.
Bertrand, M., & Guary, J. C. (2002). How plants adopt their physiology to an excess of metals. In
M. Pessarakli (Ed.), Handbook of plant and crop physiology (2nd ed., pp. 751–761). New York:
Marcel Dekker.
Bhat, V. B., & Madyastha, K. M. (2001). Scavenging of peroxynitrite by phycocyanin and phycocyanobilin from Spirulina platensis: protection against oxidative damage to DNA. Biochemical
and Biophysical Research Communications, 285, 262–266.
Biswas, A., Boutaghou, M. N., Alvey, R. M., Kronfel, C. M., Cole, R. B., Bryant, D. A., & Schluchter,
W. M. (2011). Characterization of the activities of the CpeY, CpeZ, and CpeS bilin lyases in
phycoerythrin biosynthesis in Fremyella diplosiphon strain UTEX 481. Journal of Biological
Chemistry, 286(41), 35509–35521.
Biswas, A., Vasquez, Y. M., Dragomani, T. M., Kronfel, M. L., Williams, S. R., Alvey, R. M., et al.
(2010). Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli: Chromophorylation
efficiency and specificity of all bilin lyases from Synechococcus sp. strain PCC 7002. Applied
and Environment Microbiology, 76, 2729–2739.
Blot, N., Wu, X. J., Thomas, J. C., Zhang, J., Garczarek, L., Bohm, S., et al. (2009). Phycourobilin
in trichromatic phycocyanin from oceanic cyanobacteria is formed post-transnationally by a
phycoerythrobilin lyase-isomerase. Journal of Biological Chemistry, 284, 9290–9298.
Böhm, S. B., Endres, S., Scheer, H., & Zhao, K. H. (2007). Biliprotein chromophore attachment:
Chaperone-like function of the PecE subunit of alpha-phycoerythrocyanin lyase. Journal of
Biological Chemistry, 282, 25357–25366.
Bolte, K., Kawach, O., Prechtl, J., Gruenheit, N., Nyalwidhe, J., & Maier, U. G. (2008). Complementation of a phycocyanin-bilin lyase from Synechocystis sp PCC 6803 with a nucleomorph-encoded
open reading frame from the cryptophyte Guillardia theta. BMC Plant Biology, 8, 56.
Boussiba, S., & Richmond, A. E. (1979). Isolation and characterization of phycocyanins from the
blue-green alga Spirulina platensis. Archives of Microbiology, 120, 155–159.
Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., et al. (2003). Control
of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase. Natural
Structural Biology, 10, 757–763.
Brüggemann, H., Bauer, R., Raffestin, S., & Gottschalk, G. (2004). Characterization of a
heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance. Archives of
Microbiology, 182, 259–263.
Carnicas, E., Jimenez, C., & Niell, F. X. (1999). Effects of changes of irradiances on the pigment
composition of Gracilaria tenuistipitata var. Liui Zhang et Xia. Journal of Photochemistry and
Photobiology B: Biology, 50, 149–158.
Casarett, L., & Doull, J. (1980). Toxicology (2nd ed., pp. 401–611). New York: Macmillan Publishing
Co.
Cassier-Chauvat, C., & Chauvat, F. (2015). Responses to oxidative and heavy metal stresses in
cyanobacteria: Recent advances. International Journal of Molecular Sciences, 16, 871–886.
Cervantes-Llanos, M., Lagumersindez-Denis, N., Marín-Prida, J., Pavón-Fuentes, N., FalconCama, V., Piniella-Matamoros, B., et al. (2018). Beneficial effects of oral administration of C-Phycocyanin and Phycocyanobilin in rodent models of experimental autoimmune
encephalomyelitis. Life Sciences, 194, 130–138.
Chakdar, H., & Pabbi, S. (2015). Cyanobacterial phycobilins: Production, purification, and regulation. In P. Shukla (Ed.), Frontier discoveries and innovations in interdisciplinary microbiology
(pp. 45–69). New Delhi, India: Springer.
Chaneva, G., Furnadzhieva, S., Minkova, K., & Lukavsky, J. (2007). Effect of light and temperature
on the cyanobacterium Arthronema africanum a prospective phycobiliprotein producing strain.
Journal of Applied Phycology, 19, 537–544.
Chukhutsina, V., Bersanini, L., Aro, E. M., & van Amerongen, H. (2015). Cyanobacterial
light-harvesting phycobilisomes uncouple from photosystem I during dark-to-light transitions.
Scientific Reports, 5, 14193.
Cobley, J. G., Clark, A. C., Weerasurya, S., Queseda, F. A., Xiao, J. Y., Bandrapali, N., et al.
(2002). CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the
V. K. Kannaujiya et al.
Bertrand, M., & Guary, J. C. (2002). How plants adopt their physiology to an excess of metals. In
M. Pessarakli (Ed.), Handbook of plant and crop physiology (2nd ed., pp. 751–761). New York:
Marcel Dekker.
Bhat, V. B., & Madyastha, K. M. (2001). Scavenging of peroxynitrite by phycocyanin and phycocyanobilin from Spirulina platensis: protection against oxidative damage to DNA. Biochemical
and Biophysical Research Communications, 285, 262–266.
Biswas, A., Boutaghou, M. N., Alvey, R. M., Kronfel, C. M., Cole, R. B., Bryant, D. A., & Schluchter,
W. M. (2011). Characterization of the activities of the CpeY, CpeZ, and CpeS bilin lyases in
phycoerythrin biosynthesis in Fremyella diplosiphon strain UTEX 481. Journal of Biological
Chemistry, 286(41), 35509–35521.
Biswas, A., Vasquez, Y. M., Dragomani, T. M., Kronfel, M. L., Williams, S. R., Alvey, R. M., et al.
(2010). Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli: Chromophorylation
efficiency and specificity of all bilin lyases from Synechococcus sp. strain PCC 7002. Applied
and Environment Microbiology, 76, 2729–2739.
Blot, N., Wu, X. J., Thomas, J. C., Zhang, J., Garczarek, L., Bohm, S., et al. (2009). Phycourobilin
in trichromatic phycocyanin from oceanic cyanobacteria is formed post-transnationally by a
phycoerythrobilin lyase-isomerase. Journal of Biological Chemistry, 284, 9290–9298.
Böhm, S. B., Endres, S., Scheer, H., & Zhao, K. H. (2007). Biliprotein chromophore attachment:
Chaperone-like function of the PecE subunit of alpha-phycoerythrocyanin lyase. Journal of
Biological Chemistry, 282, 25357–25366.
Bolte, K., Kawach, O., Prechtl, J., Gruenheit, N., Nyalwidhe, J., & Maier, U. G. (2008). Complementation of a phycocyanin-bilin lyase from Synechocystis sp PCC 6803 with a nucleomorph-encoded
open reading frame from the cryptophyte Guillardia theta. BMC Plant Biology, 8, 56.
Boussiba, S., & Richmond, A. E. (1979). Isolation and characterization of phycocyanins from the
blue-green alga Spirulina platensis. Archives of Microbiology, 120, 155–159.
Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., et al. (2003). Control
of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase. Natural
Structural Biology, 10, 757–763.
Brüggemann, H., Bauer, R., Raffestin, S., & Gottschalk, G. (2004). Characterization of a
heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance. Archives of
Microbiology, 182, 259–263.
Carnicas, E., Jimenez, C., & Niell, F. X. (1999). Effects of changes of irradiances on the pigment
composition of Gracilaria tenuistipitata var. Liui Zhang et Xia. Journal of Photochemistry and
Photobiology B: Biology, 50, 149–158.
Casarett, L., & Doull, J. (1980). Toxicology (2nd ed., pp. 401–611). New York: Macmillan Publishing
Co.
Cassier-Chauvat, C., & Chauvat, F. (2015). Responses to oxidative and heavy metal stresses in
cyanobacteria: Recent advances. International Journal of Molecular Sciences, 16, 871–886.
Cervantes-Llanos, M., Lagumersindez-Denis, N., Marín-Prida, J., Pavón-Fuentes, N., FalconCama, V., Piniella-Matamoros, B., et al. (2018). Beneficial effects of oral administration of C-Phycocyanin and Phycocyanobilin in rodent models of experimental autoimmune
encephalomyelitis. Life Sciences, 194, 130–138.
Chakdar, H., & Pabbi, S. (2015). Cyanobacterial phycobilins: Production, purification, and regulation. In P. Shukla (Ed.), Frontier discoveries and innovations in interdisciplinary microbiology
(pp. 45–69). New Delhi, India: Springer.
Chaneva, G., Furnadzhieva, S., Minkova, K., & Lukavsky, J. (2007). Effect of light and temperature
on the cyanobacterium Arthronema africanum a prospective phycobiliprotein producing strain.
Journal of Applied Phycology, 19, 537–544.
Chukhutsina, V., Bersanini, L., Aro, E. M., & van Amerongen, H. (2015). Cyanobacterial
light-harvesting phycobilisomes uncouple from photosystem I during dark-to-light transitions.
Scientific Reports, 5, 14193.
Cobley, J. G., Clark, A. C., Weerasurya, S., Queseda, F. A., Xiao, J. Y., Bandrapali, N., et al.
(2002). CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the
