2003
DOI: 10.1021/bi027258h
|View full text |Cite
|
Sign up to set email alerts
|

Violet Bioluminescence and Fast Kinetics from W92F Obelin:  Structure-Based Proposals for the Bioluminescence Triggering and the Identification of the Emitting Species

Abstract: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca(2+)-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca(2+), obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca(2+)] and because it emi… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

2
70
1

Year Published

2004
2004
2023
2023

Publication Types

Select...
5
2

Relationship

2
5

Authors

Journals

citations
Cited by 59 publications
(73 citation statements)
references
References 35 publications
2
70
1
Order By: Relevance
“…The substitution of Trp92 in obelin (29,30) and Trp86 (28) in aequorin, which are found not far away from the oxygen atom of the 6-(p-hydroxyphenyl) group of coelenterazine (Figure 7, right) to phenylalanine, led to the appearance of bimodal bioluminescence with a prominent contribution from the 400 nm neutral species of coelenteramide. The substitution Trp92Arg in obelin gives an almost monomodal emission around 400 nm, with almost no contribution from the excited anion (31).…”
Section: Discussionmentioning
confidence: 99%
“…The substitution of Trp92 in obelin (29,30) and Trp86 (28) in aequorin, which are found not far away from the oxygen atom of the 6-(p-hydroxyphenyl) group of coelenterazine (Figure 7, right) to phenylalanine, led to the appearance of bimodal bioluminescence with a prominent contribution from the 400 nm neutral species of coelenteramide. The substitution Trp92Arg in obelin gives an almost monomodal emission around 400 nm, with almost no contribution from the excited anion (31).…”
Section: Discussionmentioning
confidence: 99%
“…Fig. 2 shows that the crystal structure of the Ca 2ϩ -discharged protein retains the same overall scaffold as the undischarged photoprotein (18,19). The r.m.s.d.…”
Section: Overall Structure Of Camentioning
confidence: 90%
“…These are aequorin (15), obelin from Obelia longissima (16,17), and some other obelins (18,19). As expected from the homology of the primary sequences, all the photoproteins have the same compact globular structure.…”
mentioning
confidence: 82%
See 2 more Smart Citations