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Literature summary for 1.3.7.7 extracted from

  • Nomata, J.; Ogawa, T.; Kitashima, M.; Inoue, K.; Fujita, Y.
    NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters (2008), FEBS Lett., 582, 1346-1350.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ DPOR contains 7.23 mol Fe2+ per NB-protein Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Oxidation Stability

Oxidation Stability Organism
the NB-protein activity persists after the exposure to air for almost 2 h Rhodobacter capsulatus

Purification (Commentary)

Purification (Comment) Organism
protochlorophyllide-saturated NB-protein from DPOR is purified by Strep-Tactin Sepharose column chromatography Rhodobacter capsulatus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0262
-
purified enzyme, pH not specified in the publication, at 34°C Rhodobacter capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
Rhodobacter capsulatus chlorophyllide a + reduced ferredoxin + ATP
-
?

Synonyms

Synonyms Comment Organism
dark-operative Pchlide oxidoreductase
-
Rhodobacter capsulatus
dark-operative protochlorophyllide reductase
-
Rhodobacter capsulatus
DPOR
-
Rhodobacter capsulatus
light-independent protochlorophyllide oxidoreductase
-
Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center NB-protein of DPOR carries two oxygen-tolerant [4Fe–4S] clusters Rhodobacter capsulatus
ADP
-
Rhodobacter capsulatus