Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes
about
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.
P2860
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@ast
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@en
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@nl
type
label
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@ast
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@en
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@nl
prefLabel
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@ast
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@en
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@nl
P2093
P2860
P1476
Solution 1H NMR characterizati ...... ramagnetic substrate complexes
@en
P2093
Gerd N La Mar
Masaki Unno
Masao Ikeda-Saito
Zhenming Du
P2860
P304
P356
10.1016/J.JINORGBIO.2010.06.003
P577
2010-07-01T00:00:00Z