A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.
about
Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Diiron monooxygenases in natural product biosynthesis.
P2860
A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@en
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@nl
type
label
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@en
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@nl
prefLabel
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@en
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@nl
P2093
P2860
P1433
P1476
A Carboxylate Shift Regulates ...... nribosomal Peptide Synthetase.
@en
P2093
Andrew J Jasniewski
Cory J Knoot
John D Lipscomb
Lawrence Que
P2860
P304
P356
10.1021/ACS.BIOCHEM.6B00834
P407
P577
2016-09-26T00:00:00Z