Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase

Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase

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http://www.wikidata.org/entity/Q57975867
Solution structure of cytochrome b(5) mutant (E44/48/56A/D60A) and its interaction with cytochrome cNMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteriaStructural basis for cytochrome c Y67H mutant to function as a peroxidaseInvestigation of the active site of Escherichia coli Cu,Zn superoxide dismutase reveals the absence of the copper-coordinated water molecule. is the water molecule really necessary for the enzymatic mechanism?2D 1H NMR studies of oxidized 2(Fe4S4) ferredoxin from Clostridium pasteurianum.The D13C variant of Bacillus schlegelii 7Fe ferredoxin is an 8Fe ferredoxin as revealed by 1H-NMR spectroscopy.Interaction of carboxylate inhibitors with the active site of nickel(II) carboxypeptidase ASpectroscopic studies of nickel(II) carbonic anhydrase and its adducts with inorganic anionsSolution structure of oxidized microsomal rabbit cytochrome b5Transient versus steady state NOE in paramagnetic molecules Cu2 Co2 SOD as an example
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Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase

Item
http://www.wikidata.org/entity/Q57975867
description
im Dezember 1989 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в грудні 1989
@uk
name
Proton NOE studies on dicopper
@nl
Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase
@en
type
label
Proton NOE studies on dicopper
@nl
Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase
@en
prefLabel
Proton NOE studies on dicopper
@nl
Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase
@en
P1433
P1476
P304
P31
P356
P407
P433
P478
P50
P577
P356
P1433
P1476
Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase
@en
P304
P31
P356
P407
P433
P478
P50
P577