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produces a flash of light when luciferin and calcium are added, rather than the prolonged glow that is seen for luciferases when luciferin is added. In this respect, it may appear that photoproteins are not enzymes, when in fact they do
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catalytic step, which produces the light, and a slow regeneration step, where the oxyluciferin is freed and another molecule of luciferin is then enabled to bind to the enzyme. Because of the
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Photoproteins form a stable luciferin-photoprotein complex, often until the addition of another required factor such as
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worm). This was meant to distinguish them from other light-producing proteins because these do not exhibit the usual
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before it can emit light again, and this makes it appear as though it is not behaving as a typical enzyme.
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Shimomura, O. "Bioluminescence: Chemical
Principles and Methods" World Scientific Publishing Co., 2006.
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The term photoprotein was first used to describe the unusual chemistry of the luminescent system of
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Shimomura O, Johnson FH (1975). "Regeneration of the photoprotein aequorin".
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step, each aequorin molecule must "recharge" with another molecule of
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was the source of the first photoprotein to be discovered.
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Harvey, E.N. "Bioluminescence" Academic Press., 1952.
115:their bioluminescence reactions. This is due to a
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38:organisms. They add to the function of the
42:whose usual light-producing reaction is
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98:Photoproteins do not display typical
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187:1975Natur.256..236S
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181:(5514): 236–238.
94:Reaction kinetics
16:(Redirected from
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195:10.1038/256236a0
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121:kinetically slow
62:The marine worm
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46:by the enzyme
36:bioluminescent
30:are a type of
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34:produced by
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75:Chaetopterus
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65:Chaetopterus
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104:luciferases
102:as seen in
225:Categories
142:References
90:reaction.
88:luciferase
80:Polychaete
78:(a marine
48:luciferase
40:luciferins
125:luciferin
84:luciferin
44:catalyzed
236:Proteins
136:aequorin
113:catalyze
108:aequorin
211:4176627
183:Bibcode
54:History
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203:239351
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175:Nature
32:enzyme
207:S2CID
199:PMID
117:fast
191:doi
179:256
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132:Ca
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