1.3.7.3: phycoerythrobilin:ferredoxin oxidoreductase
This is an abbreviated version!
For detailed information about phycoerythrobilin:ferredoxin oxidoreductase, go to the full flat file.
Word Map on EC 1.3.7.3
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1.3.7.3
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bilins
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light-harvesting
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biliverdin
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cyanobacteria
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tetrapyrrole
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phycocyanobilin
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ferredoxin-dependent
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algae
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phycobiliproteins
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chromophore
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reductases
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phycocyanobilin:ferredoxin
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phytochromes
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heme
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open-chain
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two-electron
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phycobilins
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ixalpha
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four-electron
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cryptophytes
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apophytochrome
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d-ring
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phycobilisomes
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guillardia
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neutron
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pink
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fdbrs
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theta
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oxygenases
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peba
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biliproteins
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vinyl
- 1.3.7.3
-
bilins
-
light-harvesting
- biliverdin
- cyanobacteria
- tetrapyrrole
- phycocyanobilin
-
ferredoxin-dependent
- algae
-
phycobiliproteins
- chromophore
- reductases
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phycocyanobilin:ferredoxin
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phytochromes
- heme
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open-chain
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two-electron
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phycobilins
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ixalpha
-
four-electron
- cryptophytes
-
apophytochrome
-
d-ring
-
phycobilisomes
-
guillardia
-
neutron
-
pink
-
fdbrs
- theta
- oxygenases
-
peba
-
biliproteins
-
vinyl
Reaction
Synonyms
bilin reductase, ferredoxin:3Z-phycoerythrobilin oxidoreductase, GtPEBB, oxidoreductase, ferredoxin:3Z-phycoerythrobilin, PEB:ferredoxin oxidoreductase, PebB
ECTree
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Reaction
Reaction on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase
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(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
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(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
analysis of the reaction mechanism, after binding of 15,16-dihydrobiliverdin (DHBV) to the enzyme, Asp99 delivers a proton to the A-ring oxygen, forming a positively charged DHBVH+. After acceptance of an electron from ferredoxin, the A-ring pyrrole proton tautomerizes to the C2 position and is stabilized there. This is facilitated by the catalytic action of the axial water, which is activated/positioned by Asp219 and (indirectly) by Arg215. For the second protonation step, the reprotonation of the A-ring nitrogen, uptake of another electron, and a final tautomerization to yield the product PEB is assumed, flipped binding mode for PEB biosynthesis
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin + 2 H+
analysis of the reaction mechanism, after binding of 15,16-dihydrobiliverdin (DHBV) to the enzyme, Asp99 delivers a proton to the A-ring oxygen, forming a positively charged DHBVH+. After acceptance of an electron from ferredoxin, the A-ring pyrrole proton tautomerizes to the C2 position and is stabilized there. This is facilitated by the catalytic action of the axial water, which is activated/positioned by Asp219 and (indirectly) by Arg215. For the second protonation step, the reprotonation of the A-ring nitrogen, uptake of another electron, and a final tautomerization to yield the product PEB is assumed, flipped binding mode for PEB biosynthesis
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