Extending the motif of the [FeFe]-hydrogenase active site models: protonation of Fe2(NR)2(CO)6-xLx species.
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The Mechanism of N-N Double Bond Cleavage by an Iron(II) Hydride ComplexDi/mono-nuclear iron(I)/(II) complexes as functional models for the 2Fe2S subunit and distal Fe moiety of the active site of [FeFe] hydrogenases: protonations, molecular structures and electrochemical properties.Bridging-hydride influence on the electronic structure of an [FeFe] hydrogenase active-site model complex revealed by XAES-DFT.Azo group(s) in selected macrocyclic compounds.
P2860
Extending the motif of the [FeFe]-hydrogenase active site models: protonation of Fe2(NR)2(CO)6-xLx species.
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2007年の論文
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name
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@ast
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@en
type
label
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@ast
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@en
prefLabel
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@ast
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@en
P2860
P1476
Extending the motif of the [Fe ...... of Fe2(NR)2(CO)6-xLx species.
@en
P2093
Phillip I Volkers
Thomas B Rauchfuss
P2860
P304
P356
10.1016/J.JINORGBIO.2007.05.005
P577
2007-05-24T00:00:00Z