MG_229_231_TETRAMER_ox – oxidized ribonucleoside-diphosphate reductase

Name
WID MG_229_231_TETRAMER_ox View in model
Name oxidized ribonucleoside-diphosphate reductase View in model
 
Structure
Biosynthesis [c]: MG_229_231_TETRAMER + O2 ⇒ (4) H + MG_229_231_TETRAMER_ox View in model
No. subunits 0
Disulfide bonds (pH 7.5) View in model
Empirical formula (pH 7.5) H16936C11020N2820O3238S66
Molecular weight (pH 7.5; Da) 242848.95 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
283530.00
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1199.86 View in model
 
Synthesis
Formation process Process_Metabolism View in model
Localization c
 
Function
Reaction participant View in model
Complex subunit oxidized ribonucleoside-diphosphate reductase
[c]: MG_229_231_TETRAMER + O2 ⇒ (4) H + MG_229_231_TETRAMER_ox
View in model
 
Comments
Comments During catalytic cycle NrdEF complex obtains [PUB_0160] oxygen coordinated to tryosine 126 of beta subunit (NrdF, MG_229) disulfide bonds between C176 and C413 of alpha subunit (NrdE, MG_231) NrdEF is recycled by [PUB_0160] NrdI removes NrdF oxygens NrdH (or Trx in organisms such as M. genitalium which lack NrdH) reduces NrdE disulfide bonds
References
  1. Cotruvo JA Jr, Stubbe J. NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Proc Natl Acad Sci U S A 105, 14383-8 (2008). WholeCell: PUB_0160, PubMed: 18799738

 
Metadata
Created 2012-10-01 15:07:39
Last updated 2012-10-01 15:14:10